Method of obtaining polymer-containing fibres

FIELD: chemistry.

SUBSTANCE: invention relates to method of spinning fibre, containing polypeptide polymer, as well as to products, including said polymer fibre. Method of fibre spinning includes draft of fibre from dope solution, containing polymer, preferably silk polypeptide which can be introduced into water solution with concentration constituting at least 0.15 mg/ml, polyacrylamide (PAA), which increases longitudinal viscosity of dope solution, and solvent. Invention makes it possible to obtain fibres, including living and non-living biological material, which could perform function of framework material for fabric engineering and growing artificial organs.

EFFECT: application of PAA in dope solution results in obtaining smooth and homogeneous fibres, non-biodegradable and long-lasting, in addition, application of very low concentrations of polymers and/or very low concentrations of improvers of PAA longitudinal viscosity facilitates spinning of fibres from dope solution.

24 cl, 4 dwg, 7 ex

 

The present invention relates to a method for spinning a polymer fiber. Furthermore, it relates to polymeric fiber obtained by the above method, and variants of its application. The invention also relates to products, incorporating the polymer fiber.

The level of technology

Conventional methods for producing polymer fibers characteristic of significant shortcomings in respect of both methods and products. K methods usually are requirements, excessively hard to turn on biological material such as proteins or cells, in terms of conditions relating to temperature, pressure or the use of chemicals and solvents. Products are usually developed to demonstrate superiority in one property, such as strength, elasticity or weight. However, the Union of all these properties was difficult.

Natural spider silk can take different forms depending on the gland, in which it is formed (Gosline et al., J. Exp. Biol. (202): 3295, 1999). Its properties are worthy of attention: it is the limit of the tensile strength can exceed the appropriate response of steel and to be equal to the limit of the tensile strength aramid elementary fibers such as Kevlar brand. The spider silk can also be very pliable being extendable up to approx�an astounding 300% of its length without breaking. Among other things, it is light in weight.

Since the generation of native spider silk is impractical due to territorial and cannibalistic nature of spiders, scientific and commercial interest initiated the study of the manufacture of artificial silk spider for possible obtain on an industrial scale. However, finding commercially competitive way of mass production of spider silk has proved difficult. Artificial receiving faced with the problems of achieving sufficient protein output and quality of build threads. To a solution of a protein source is directed to the preparation of recombinant proteins in spider silk when using bacteria (Scheibel, Microb. Cell. Fact., (1): 14, 2004). However, drawing fibers from aqueous solutions of these proteins is impossible, because such a solution, by itself, does not demonstrate sufficient longitudinal strength.

The hair is a way of deforming stresses in the direction of the fibre axis compete with surface tension of the spinning syrup. For example, it is impossible to pull a stable fluid elementary fiber from the water due to the high surface tension of water.

This illustrates the Rayleigh instability, which causes destruction of the jet of water, which water is flowing from�wired crane, on the droplets. This effect is called surface tension of water.

The ratio between viscous forces and surface tension describes the number Ohnesorg Oh.

Oh=ηρσR

A small value of the number of Oh (Oh<<1) means that a fluid elementary fiber will disintegrate into small droplets, which stimulates the surface tension. The importance of Oh number means that a fluid elementary fiber will remain stable (Edmond, Schofield et al. 2006). In effect this means that spinning syrup should demonstrate the importance of the number Ohnesorg. Obviously, the value of the number of Oh can be increased by increasing the viscosity. In fluids, characterized by a high coefficient of crotona in the processes of the longitudinal currents will dominate longitudinal viscosity and therefore large values of the number of Oh can be achieved for flowing media, which are characterized by relatively low shear viscosity η, but a high coefficient of crotona Tr.

Recombinant protein of spider silk can be obtained by using bacteria, its Assembly was investigated in detail (Scheibel, Microb. Cell. Fact., (1): 14, 2004; Huemmerich et al., Curr. Biol., (22): 2070-4, 2004; Rammensee et al., PNAS, (105):659-6595, 2008). Artificial spinning syrups having a low concentration of protein (10-20 mg/ml eADF3 and eADF4), do not detect the ratio Tr>>1. Surface tension is still far greater than the effects of viscosity, thus, also has a place and Oh<<1, so getting the fiber from these solutions having a low concentration of protein was impossible. Fiber provided only solutions recombinant protein of spider silk that has a very high concentration of protein (~200 mg/ml), (Exier et al., Angewandte Chemie-Intemational Edition, (19): 3559-3562, 2007). However, the increase in the concentration of the protein leads to an increase in shear viscosity of the solution, and the processability of the fluid, characterized by very high (>1 PA-s) shear viscosity, is pretty bad.

The inventors of the present invention, to his surprise, found that for spinning fibers by the method of the present invention requires only very low concentrations of polymer. The use of very low concentrations of polymer inherent advantage in the absence of increased shear viscosity of the solution, which in turn improves the processability of the fluid medium.

Surprisingly, receiving fibers from a very low concentration of polymers, such as silk polypeptides, such as polypeptides spider silk in soft conditions� facilitated by the inclusion of improvers longitudinal viscosity. Although spinning syrups spider silk in their nature and were described as characterized by very high interest levels of a protein of spider silk, the real way, surprisingly, requires the use of only very low concentrations of silk polypeptides, ranging from concentrations constituting only 0.15 mg/ml.

Furthermore, this method, surprisingly, requires the use of only very low concentrations of the above-mentioned improvers longitudinal viscosity. Low concentrations mentioned improvers, on the one hand, sufficient to increase the longitudinal viscosity of the solution, but, on the other hand, substantially no increase of the shear viscosity of the solution, so that the formation of fibers is improved.

Thus, the use of very low concentrations of polymers and/or very low concentrations of improvers longitudinal viscosity in the method of the present invention facilitates the spinning of fibers from a spinning solution. In addition, the technical obstacles in the way are small, they do direct extraction of fibers from the solution of the silk polypeptide in environmental conditions or conditions close to him.

Summary of invention

In a first aspect the present invention relates to a method of spinning fibers from a spinning solution comprising the stage of:

(a) �of Holocene spinning solution, containing (i) a polymer that can be put into aqueous solution with concentration, component, at least 0.15 mg/ml, (ii) a compound that increases the elongation viscosity of the spinning solution, and (iii) a solvent; and

(b) drawing the fiber from a spinning solution or combination of extrusion and drawing fibers from a spinning solution, to thereby produce a fiber.

In a second aspect, the present invention relates to a spinning solution for implementing the method of the present invention containing (i) a polymer that can be put into aqueous solution with concentration, component, at least 0.15 mg/ml, (ii) a compound that increases the elongation viscosity of the spinning solution, and (iii) a solvent.

In the third aspect the present invention relates to fiber obtained by the method of the first aspect, and to its use.

In a fourth aspect the present invention provides products comprising fiber of the second aspect.

This summary of the invention does not necessarily describe all features of the invention.

A detailed description of the invention

Before bringing the following detailed description of the present invention should be understood that this invention is not limited to the particular methodology, protocols, and reagents described in this document.�those because they can vary. It is also necessary to understand what the terminology is in accordance with the usage in this document is intended only for the purpose of describing particular embodiments and is not meant to limit the scope of the present invention, which will be limited only by the appended claims of the invention. Unless another, all technical and scientific terms in accordance with the usage in this document have the same meaning as generally understood by experts in the relevant field of technology.

Preferably, the terms in accordance with the usage in this document are defined according to the description in the publication "A multilingual glossary of biotechnological terms: (IUPAC Recommendations)", Leuenberger, H. G. W., Nagel, B. and Kölbl, H. eds. (1995), Helvetica Chemie Acta, CH-4010 Basel, Switzerland).

Throughout the text of this description of the invention cited several documents. Each of the documents cited herein (including all patents, applications for patents, scientific publications, technical descriptions from the manufacturer, instructions, views, sequences with GenBank access numbers and the like), whether above or below herein in its entirety by reference is incorporated herein. Nothing in us�Mr sage document should not be construed as an assumption of a that the invention is not entitled to the claimed date of priority on the basis of the priority application.

In the following will be described elements of the present invention. These elements are listed together with the specific choices of implementation, however, it should be understood that additional embodiments they can be combined in any manner and in any quantity. Different manner described in the examples and preferred options for implementation should not be construed as limiting the present invention just described variants of implementation. This description of the invention should be understood as justifying and covering implementation options that combine the detailed options for the implementation of any number of the described and/or preferred elements. In addition, disclosed in the description of the present application should be considered any permutation and combination of all elements described in this application, unless the context otherwise will point to another.

In the course of presentation of the description of the invention and of the claims which follows, unless the context otherwise would require another, the word "include" and variations such as "comprises" and "comprising" will be understood to imply the inclusion�of the specified integer or stage or group of integers or steps but not the exclusion of any other integer or stage or group of integers or steps.

In accordance with the use in this description and the appended claims, the singular form (for example, one, some and present) include the plural, unless the content clearly will not dictate the other.

Residues in two or more polypeptides are considered to be "related" to each other, if the remains occupy a similar position in the polypeptide structures. As is well known at the present level of technology, similar provisions in two or more polypeptides can be identified by alignment of the polypeptide sequences based on the amino acid sequence similarity or structural similarity. Funds for such alignment experts in the relevant field of technology is well known and can for example be obtained on the Internet, for example, ClustalW (www.ebi.ac.uk/clustalw) or Align (http://www.ebi.ac.uk//emboss/align/index.html) when using standard installations, it is preferable to EMBOSS alignment: needle, Matrix: Blosum62, the Penalty for opening a gap: 10.0, the Penalty for the continuation gap 0.5.

In a first aspect the present invention relates to a method of spinning fibers from a spinning solution comprising, essentially consisting of, or consisting of seq�blowing stages:

(a) obtain a spinning solution containing (i) a polymer that can be put into aqueous solution with concentration, component, at least 0.15 mg/ml, (ii) a compound that increases the elongation viscosity of the spinning solution, and (iii) a solvent; and

(b) drawing the fiber from a spinning solution or combination of extrusion and drawing fibers from a spinning solution, to thereby produce a fiber.

In the context of the present invention the term "polymer" refers to a molecule formed from a repeating structural units typically connected by covalent chemical bonds.

In one preferred embodiment of the polymer is a biopolymer, such as a polypeptide or a synthetic polymer.

The term "biopolymer" in accordance with the usage in this document refers to a molecule comprising monomer units that are covalently linked to form larger structures. Biopolymers in the classification can be divided into three main classes on the basis of differing monomer units used and the structure of the obtained biopolymers. The first class of biopolymers is the polynucleotides, which are polymers formed from nucleotide monomers, such as polymers formed from 10 or more� nucleotide monomers. The second class of biopolymer is a polypeptide, which are polymers of amino acids. The third class of biopolymer is a polysaccharide, which are often associated linear polymeric carbohydrate structures. Is preferred that the biopolymer would represent a polypeptide.

Preferably, the biopolymer is biodegradable, and more preferably also compostable. Biodegradable biopolymers decompose to COz and water under the action of microorganisms. Biodegradable biopolymers that are also compostable, can be put in the way of industrial composting and will decompose over a period of months.

Also is preferred that the biopolymer would be biocompatible. This means that the polymer is non-toxic, by not mutagen and causes zero or only minimal inflammatory response.

Thus, and also fibers, spun from biopolymers according to the method of the present invention can exhibit the above-mentioned advantageous features, namely can be biodegradable, compostable and/or biocompatible or can be substantially biodegradable, compostable and/or biocompatible. In particular, since the number improvers longitudinal viscosity in the spinning solution method n�standing of the invention is preferably very low.

As mentioned above, the polypeptide of the recurring structural units are amino acids connected by covalent amide bonds (peptide bonds).

Unless otherwise stated, the terms "polypeptide" and "protein" are used herein interchangeably and refer to any polysaccharide-linked chain of amino acids, regardless of length or post-translational modification.

Preferably the polypeptide are the silk polypeptide comprising at least two identical repetitive element, bovine serum albumin (BSA), Zein or casein. The polypeptide may also be a collagen, fibronectin or keratin.

Bovine serum albumin (BSA), also known as "Fraction V", is a serum albumin protein. Zein is preliminaly a protein found in corn. Casein (from Latin caseus "cheese") is a predominant phosphoprotein (αS1, αS2, β, κ), which is responsible for nearly 80% of proteins in cow's milk and cheese.

In the context of the present invention, the term "silk polypeptide" refers to a polypeptide or protein of the silk (it should be noted that unless otherwise stated, these two terms are in accordance with the usage in this document are used interchangeably) which Express in a recombinant expression system (for example, microorganisms, yeasts, plants, insects or mammals), that is, separated from its natural environment in the iron spider (recombinant polypeptide or protein of silk). Preferably, the silk polypeptide" is isolated or purified. In particular, the "treated silk polypeptide" or "polypeptide selected silk" is free or substantially free of cellular material or other contaminating proteins from the cell or tissue source from which the protein is isolated or produced. The term "substantially free of cellular material" includes preparations of the polypeptide of silk, in which the silk polypeptide is separated from cellular components of the cells from which it recombinante get. Thus, the silk polypeptide that is substantially free of cellular material includes preparations of the polypeptide of silk, containing less than approximately 30%, 20%, 10%, 5% or 1% (based on dry weight) of contaminating protein. In the case of the expression of the silk polypeptide in cell culture it will also be free or substantially free of culture medium, that is, the culture medium will be less than approximately 20%, 10%, 5% or 1% of the volume of the polypeptide preparation.

"The silk polypeptide in accordance with the context of the present invention additionally relates to the polyp�the TTI, comprising the amino acid sequence that comprises or consists of at least, 50%, 60%, 65%, 70%, 75%, 80%, 85%, 90%, preferably, at least 95%, and most preferably 100%, multiple identical copies of the same repetitive element (e.g. A2, Q6or C16where positions 2, 6 or 16 represent the number of repeating units) or multiple copies of two or more different repeating units (for example, (AQ)24or (AQ)12, C16).

The terms "duplicate link" and "link retry" in the context of the present invention can be used interchangeably,

In the context of the present invention, the term "silk polypeptide" also refers to the silk polypeptide, which comprises or consists of at least two identical repetitive units which comprise or consist of identical copies of the amino acid sequences of the polypeptides of silk found in nature, or variations of amino acid sequences of the polypeptides of silk found in nature, or combinations of both.

In the context of the present invention "duplicate link" refers to a region in which the amino acid sequence corresponds to a region that includes or consists of at least one peptide motif (e.g.�measures AAAAAA (SEQ ID NO:13) or GPGQQ (SEQ ID NO:4)), which is repeated in the silk polypeptide found in nature, (for example, MaSpI, ADF-3, ADF-4, or Flag) (i.e. identical to the amino acid sequence), or to the amino acid sequence essentially similar to it (i.e. to the variant amino acid sequence). In this regard, the term "substantially similar" refers to the degree of amino acid identity, at least for 50%, 51%, 52%, 53%, 54%, 55%, 56%, 57%, 58%, 59%, 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or even to 99.9%, preferably over the entire length corresponding to a reference amino acid sequence found in nature. "Duplicate" link in the chain comprising the amino acid sequence that is "substantially similar" corresponding amino acid sequence in the silk polypeptide found in nature (i.e. duplicate link wild-type), is also similar in respect to their functional properties, for example, the silk polypeptide comprising the "substantially similar duplicate link", still has the ability to form a fiber. Preferably from the silk polypeptide comprising the "substantially similar duplicate link", it is still possible to extract GLA�whom and homogeneous fiber at a speed, component of at least 0.1 cm/sec, preferably 10 cm/sec, and more preferably 10 m/sec. A specialist in the relevant field of technology can perform a visual assessment will still be receiving fiber. Smooth and uniform appearance mentioned fiber can be monitored using electron microscopy.

"Duplicate" link in the chain comprising the amino acid sequence that is "identical" amino acid sequence of the polypeptide of silk found in nature, for example, may constitute a part of the silk polypeptide corresponding to one or more peptide motifs MaSpI (SEQ ID NO:43), MaSpII (SEQ ID NO:44), ADF-3 (SEQ ID NO:1) and/or ADF-4 (SEQ ID NO:2). "Duplicate" link in the chain comprising the amino acid sequence that is "substantially similar" amino acid sequence of the polypeptide of silk found in nature, for example, may constitute a part of the silk polypeptide corresponding to one or more peptide motifs MaSpI (SEQ ID NO:43), MaSpII (SEQ ID NO:44), ADF-3 (SEQ ID NO:1) and/or ADF-4 (SEQ ID NO:2), but which includes one or more amino acid substitutions at specific amino acid positions.

"Duplicate link" does not include non-repetitive hydrophilic amino acid domain, in the General case, presumably Pris�according to the carboxy - and amino-ends of the silk polypeptides, found in nature.

"Duplicate link" in accordance with the present invention further relates to the amino acid sequence, having a length of from 3 to 200 amino acids, or from 5 to 150 amino acids, preferably having a length of from 10 to 100 amino acids, or from 15 to 80 amino acids, and more preferably having a length of from 18 to 60 amino acids, or from 20 to 40 amino acids. For example, a recurring element corresponding to the present invention may have a length of 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, 49, 50, 51, 52, 53, 54, 55, 56, 57, 58, 59, 60, 61, 62, 63, 64, 65, 66, 67, 68, 69, 70, 71, 72, 73, 74, 75, 76, 77, 78, 79, 80, 81, 82, 83, 84, 85, 86, 87, 88, 89, 90, 91, 92, 93, 94, 95, 96, 97, 98, 99, 100, 105, 110, 115, 120, 125, 130, 135, 140, 145, 150, 155, 160, 165, 170, 175, 180, 185, 190, 195 or 200 amino acids. Most preferably a repeating unit, corresponding to the invention, consists of 3, 4, 5, 6, 7, 8, 9, 10, 12, 15, 18, 20, 24, 27, 28, 30, 31, 32, 33, 34, 35, 36, 37, 38 or 39 amino acids.

The silk polypeptide used in the method of the present invention, preferably consists of amino acids in an amount of from 6 to 1500, amino acids in an amount of from 50 to 1500 or amino acid in an amount of from 200 to 1300, and most preferably the amino acids in an amount of from 250 to 1200 or amino acid number of from 500 to 1000.

Preferably, the silk polypeptide used in the method of the present Fig�t, includes or consists of 2-80 repeating units, 3-80 repeating units or 4-60 repeating units, more preferably between 8 to 48 repetitive units, or between 10 to 40 repetitive units and most preferably between 16 to 32 repetitive units. For example, the silk polypeptide used in the method of the present invention, may include or be composed of: 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, 49, 50, 51, 52, 53, 54, 55, 56, 57, 58, 59, 60, 61, 62, 63, 64, 65, 66, 67, 68, 69, 70, 71, 72, 73, 74, 75, 76, 77, 78, 79 or 80 repeating units. Most preferably, the silk polypeptide comprises 4, 8, 12, 16, 24, 32 or 48 repeating units. As mentioned above, at least two repetitive element that is included in the silk polypeptide used in the method of the present invention, are identical to the repeating unit. Thus, the silk polypeptide used in the method of the present invention, may include multiple copies of identical repetitive element (e.g. A2or C16where positions 2 or 6 represent the number of repeating units) or multiple copies of two or more different repeating units (for example, (AQ)24or (QAQ)8). For example. 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40,41, 42, 43, 44, 45, 46, 47, 48, 49, 50, 51, 52, 53, 54, 55, 56, 57, 58, 59, 60, 61, 62, 63, 64, 65, 66, 67, 68, 69, 70, 71, 72, 73, 74, 75, 76, 77, 78, 79 or 80 of 80 repeating units that may be included in the silk polypeptide used in the method of the present invention, are identical to the repeating unit.

The silk polypeptide used in the method of the present invention, may include or consist of the amino acid sequence of any polypeptide of silk, known to those skilled in the art. Is preferred that the silk polypeptide used in the method of the present invention, includes or consists of the amino acid sequence of the polypeptide silk insect, preferably the polypeptide of arthropod or polypeptide of spider silk. The silk polypeptide used in the method of the present invention, may also include or consist of the amino acid sequence of the polypeptide silk mytilid.

Is preferred that the silk polypeptide spider includes or consists of the amino acid sequence of the polypeptide great inuloides cancer (MaSp), such as a polypeptide cord threads of spider silk, small polypeptide inuloides cancer (MiSp), polypeptide hunting helical filaments (flagelliform), polypeptide spider silk from a tree cancer (aggregate), polypeptide spider silk from Golikov�ne cancer (aciniform) or polypeptide of spider silk from Piriform gland (pyriform). Most preferably, the silk polypeptide spider comprises or consists of the amino acid sequence of the polypeptide of spider silk cord threads or polypeptide silk spider hunting helical filaments. In the General case is preferred that the amino acid sequence of the polypeptide cord threads or polypeptide hunting helical thread would have been a polypeptide selected from the cord threads or polypeptide hunting helical threads of Orb-web spiders Araneidae or Araneoid.

Is preferred that the silk polypeptide of the insect off would or would consist of the amino acid sequence of the polypeptide silk Lepidoptera. More preferably, the silk polypeptide of the insect comprises or consists of the amino acid sequence of the polypeptide silk Bombycidae, most preferably Bombyx mori.

Preferably, the above-mentioned polypeptides silk obtained recombinant, which are recombinant polypeptides of silk. For example, the silk polypeptides used in the method of the present invention are recombinant polypeptides of spider silk, such as polypeptides spider silk cord threads or polypeptides silk spider hunting helical filaments, recombinant polypeptides of silk insect or recombinant polypeptides silk mytilid.

A recurring element of the polypeptide was�and, used in the method of the present invention, may include or consist of the amino acid sequence of any area which includes or consists of at least one peptide motif that is repeated in occurring the silk polypeptide, are known to those skilled in the art. Preferably the repeating element of the silk polypeptide used in the method of the present invention comprises or consists of the amino acid sequence region that comprises or consists of at least one peptide motif that is repeated in the silk polypeptide of the insect, more preferably the polypeptide of arthropod silk or silk polypeptide spider. A recurring element of the silk polypeptide used in the method of the present invention, may also include or consist of the amino acid sequence region that comprises or consists of at least one peptide motif that is repeated in the silk polypeptide mytilid.

It is preferable to duplicate the link of spider silk would include or consists of the amino acid sequence region that comprises or consists of at least one peptide motif,�which the repeating image is present in naturally occurring the polypeptide great inuloides cancer (MaSp), such as a polypeptide of spider silk cord threads, the small polypeptide inuloides cancer (MiSp), the polypeptide hunting helical filaments, the polypeptide of spider silk from a tree glands, the polypeptide of spider silk from delavenay cancer or polypeptide spider silk from a pear-shaped gland. Most preferably the repeating element comprises or consists of the amino acid sequence region that comprises or consists of at least one peptide motif that is repeated in occurring the polypeptide of spider silk cord threads or polypeptide silk spider hunting spiral threads.

It is preferable to duplicate the link silk insect would include or consists of the amino acid sequence region that comprises or consists of at least one peptide motif that is repeated in occurring the silk polypeptide Lepidoptera. More preferably, the recurring link silk insect comprises or consists of the amino acid sequence region that comprises or consists of at least one peptide motif that is repeated in occurring the silk polypeptide insect Bombycidae, most preferably Bombyx mori.

The term "opener�Sosna sequence in accordance with the use in the context of the present invention relates to the amino acid sequence, which includes amino acids, which are often present in a certain position (for example, "G") and where other amino acids that do not specify additionally, replace the symbol-placeholder "X".

Preferably, the silk polypeptide used in the method of the present invention comprises, essentially consists of or consists of at least two identical repeating units, each of which includes at least one, preferably one, a consensus sequence selected from the group consisting of:

(i) GPGXX (SEQ ID NO:3), where X represents any amino acid, preferably in each case independently selected from A, S, G, Y, P, N and Q;

(ii) GGX, where X represents any amino acid, preferably in each case independently selected from Y, P, R, S, A, T, N and Q, more preferably in each case independently selected from Y, P and Q; and

(iii) Axwhere x is an integer in the range from 5 to 10.

Also is preferred that the silk polypeptide used in the method of the present invention would or would consist of at least two identical repeating units, each of which includes at least one, preferably one, amino acid sequence selected from the group consisting of: GGRPSDTYG (SEQ ID NO:18) and GGRPSSSYG (SEQ ID NO:19).

P�Vtorushina (peptide) GPGXX motifs (SEQ ID NO:3) and GGX, that is, motifs enriched in glycine, give flexibility to the silk polypeptide and, thus, the threads obtained from silk protein comprising mentioned motives. Speaking in detail, a recurring motif GPGXX (SEQ ID NO:3) forms a helical structure of β-turn, which give the silk polypeptide elasticity. As the great silk inuloides glands and silk hunting helical filaments include motive GPGXX (SEQ ID NO:3). Duplicate GGX motif is associated with spiral structure including three amino acids in a single turn, and occurs in the majority of spider silks. GGX motif can give additional silk elastic properties. Duplicate polyalanine Andx(peptide) motif forms a crystalline structure β-sheet, which gives the silk polypeptide strength, (WO 03/057727). (Peptide) motives GGRPSDTYG (SEQ ID NO:18) and GGRPSSSYG (SEQ ID NO:19) were selected from resilin (WO 08/155304). Resilin is an elastomeric protein found in most arthropods (arthropodd). He is in specialized areas of the cuticle, giving low stiffness and high strength (Elvin et al. Nature(473): 999-1002, 2005).

Thus, in one preferred embodiment of the present invention, the silk polypeptide comprises or consists of repeating units, each of which 14 includes at least one (for example, 1, 2, 3, 4, 5, 6, 7, 8, or 9), preferred�Stateline one, amino acid sequence selected from the group consisting of GPGAS (SEQ ID NO:5), GPGSG (SEQ ID NO:6), GPGGY (SEQ ID NO:7). GPGGP (SEQ ID NO:8), GPGGA (SEQ ID NO:9), GPGQQ (SEQ ID NO:4), GPGGG (SEQ ID NO:10), GPGQG (SEQ ID NO:40) and GPGGS (SEQ ID NO:11). In yet another preferred embodiment of the present invention, the silk polypeptide comprises or consists of repeating units, each of which includes at least one (for example, 1, 2, 3, 4, 5, 8, 7 or 8), preferably one, amino acid sequence selected from the group consisting of GGY, GGP, GGA, GGR, GGS, GGT, GGN and GGQ. In one additional preferred embodiment of the present invention, the silk polypeptide comprises or consists of repeating units, each of which includes at least one (for example, 1, 2, 3, 4, 5 or 6), preferably one, amino acid sequence selected from the group consisting of AAAA (SEQ ID NO:12), AAAAAA (SEQ ID NO:13), AAAAAAA (SEQ ID NO:14), AAAAAAAA (SEQ ID NO:15), AAAAAAAAA (SEQ ID NO:16) and AAAAAAAAAA (SEQ ID NO:17).

In yet another preferred embodiment, the silk polypeptide comprises or consists of repeating units, each of which includes at least one (for example, 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24 or 25), preferably one, amino acid sequence selected from the group consisting of GPGAS (SEQ ID NO:5), GPGSG (SEQ ID NO:6), GPGGY (SEQ ID NO:7), GPGGP (SEQ D NO:8), GPGGA (SEQ ID NO:9), GPGQQ (SEQ ID NO:4), GPGGG (SEQ ID NO:10), GPGQG (SEQ ID NO:40), GPGGS (SEQ ID NO:11), GGY, GGP, GGA, GGR, GGS, GGT, GGN, GGQ, AAAA (SEQ ID NO:12), AAAAAA (SEQ ID NO:13), AAAAAAA (SEQ ID NO:14), AAAAAAAA (SEQ ID NO:15), AAAAAAAAA (SEQ ID NO:16), AAAAAAAAAA (SEQ ID NO:17), GGRPSDTYG (SEQ ID NO:18) and GGRPSSSYG (SEQ ID NO:19).

Most preferably, the silk polypeptide used in the method of the present invention comprises, essentially consists of or consists of repetitive units which comprise or consist of:

(i) GPGAS (SEQ ID NO:5), AAAAAA (SEQ ID NO:13), GGY and GPGSG (SEQ ID NO:6) as amino acid sequence, preferably in this order,

(ii) AAAAAAAA (SEQ ID NO:15), GPGGY (SEQ ID NO:7), GPGGY (SEQ ID NO:7) and GPGGP (SEQ ID NO:8) as amino acid sequence, preferably in this order,

(iii) GPGQQ (SEQ ID NO:4), GPGQQ (SEQ ID NO:4), GPGQQ (SEQ ID NO:4) and GPGQQ (SEQ ID NO:4) as the amino acid sequence, preferably in this order,

(iv) GPGGA (SEQ ID NO:9), GGP, GPGGA (SEQ ID NO:9), GGP, GPGGA (SEQ ID NO:9) and GGP as the amino acid sequence, preferably in this order,

(v) AAAAAAAA (SEQ ID NO:15),GPGQG (SEQ ID NO:40) and GGR as the amino acid sequence, preferably in this order,

(vi) AAAAAAAA (SEQ ID NO:15), GPGGG (SEQ ID NO:10), GGR, GGN and GGR as the amino acid sequence, preferably in this order,

(vii) GGA, GGA, GGA, GGS, GGA and GGS as the amino acid sequence, preferably in this order,

(viii) GPGGA (SEQ ID NO:9), GPGGY SEQ ID NO:7), GPGGS (SEQ ID NO:11), GPGGY (SEQ ID NO:7), GPGGS (SEQ ID NO:11) and GPGGY (SEQ ID NO:7) as amino acid sequence, preferably in this order.

It should be noted that at least two of the repetitive element that is included in the above-mentioned polypeptides silk, are identical to the repeating unit.

Preferably, the silk polypeptide used in the method of the present invention comprises, essentially consists of or consists 2-80 repeating units, 3-80 repeating units or 4-60 repeating units, more preferably between 8 to 48 repetitive units, or between 10 to 40 repetitive units and most preferably between 16 to 32 repetitive units, that is, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, 49, 50, 51, 52, 53, 54, 55, 56, 57, 58, 59, 60, 61, 62, 63, 64, 65, 66, 67, 68, 69, 70, 71, 72, 73, 74, 75, 76, 77, 78, 79 or 80 repeating units, each of which includes at least one, preferably one, a consensus sequence selected from the group consisting of:

(i) GPGXX (SEQ ID NO:3), where X represents any amino acid, preferably in each case independently selected from A, S, G, Y, P, N and Q;

and) GGX, where X represents any amino acid, preferably in each case independently selected from Y, P, R, S, A, T, N and Q, more preferably in each�m case independently selected from Y, P and Q; and

(iii) Axwhere x is an integer in the range from 5 to 10.

As mentioned above, at least two repetitive element that is included in the silk polypeptide used in the method of the present invention, are identical to the repeating unit.

Also is preferred that the silk polypeptide used in the method of the present invention would or would consist of 2-80 repeating units, 3-80 repeating units or 4-60 repeating units, more preferably between 8 to 48 repetitive units, or between 10 to 40 repetitive units and most preferably between 16 to 32 repetitive units, each of which includes at least one, preferably one, amino acid sequence selected from the group consisting of: GGRPSDTYG (SEQ ID NO:18) and GGRPSSSYG (SEQ ID NO:19).

Thus, the silk polypeptide used in the method of the present invention, preferably comprises, essentially consists of or consists 2-80 repeating units, 3-80 repeating units or 4-60 repeating units, more preferably between 8 to 48 repetitive units, or between 10 to 40 repetitive units and most preferably between 16 to 32 repetitive units, each of which includes at least one (for example, 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24 and�and 25), preferably one, amino acid sequence selected from the group consisting of GPGAS (SEQ ID NO:5), GPGSG (SEQ ID NO:6), GPGGY (SEQ ID NO:7), GPGGP (SEQ ID NO:8), GPGGA (SEQ ID NO:9), GPGQQ (SEQ ID NO:4), GPGQG (SEQ ID NO:40), GPGGG (SEQ ID NO:10), GPGGS (SEQ ID NO:11), GGY, GGP, GGA, GGR, GGS, GGT, GGN, GGQ, AAAAA (SEQ ID NO:12), AAAAAA (SEQ ID NO:13), AAAAAAA (SEQ ID NO:14), AAAAAAAA (SEQ ID NO:15), AAAAAAAAA (SEQ ID NO:16), AAAAAAAAAA (SEQ ID NO:17), GGRPSDTYG (SEQ ID NO:18) and GGRPSSSYG (SEQ ID NO:19).

Most preferably, the silk polypeptide used in the method of the present invention comprises, essentially consists of or consists of:

(i) repeating units which comprise or consist of: GPGAS (SEQ ID NO:5), AAAAAA (SEQ ID NO:13), GGY and GPGSG (SEQ ID NO:6) as amino acid sequence, preferably in this order,

(ii) repeating units which comprise or consist of: AAAAAAAA (SEQ ID NO:15), GPGGY (SEQ ID NO:7), GPGGY (SEQ ID NO:7) and GPGGP (SEQ ID NO:8) as amino acid sequence, preferably in this order,

(iii) repeating units which comprise or consist of: GPGQQ (SEQ ID NO:4), GPGQQ (SEQ ID NO:4), GPGQQ (SEQ ID NO:4) and GPGQQ (SEQ ID NO:4) as the amino acid sequence, preferably in this order,

(iv) repeating units which comprise or consist of: GPGGA (SEQ ID NO:9), GGP, GPGGA (SEQ ID NO:9), GGP, GPGGA (SEQ ID NO:9) and GGP as the amino acid sequence, preferably in this order,

(v) repeating units which comprise or consist of: AAAAAAAA (SEQ I NO:15),GPGQG (SEQ ID NO:40) and GGR as the amino acid sequence, preferably in this order,

(vi) repeating units which comprise or consist of: AAAAAAAA (SEQ ID NO:15), GPGGG (SEQ ID NO:10), GGR, GGN and GGR as the amino acid sequence, preferably in this order,

(vii) repeating units which comprise or consist of: GGA, GGA, GGA, GGS, GGA and GGS as the amino acid sequence, preferably in this order, and/or

(viii) repeating units which comprise or consist of: GPGGA (SEQ ID NO:9), GPGGY (SEQ ID NO:7), GPGGS (SEQ ID NO:11), GPGGY (SEQ ID NO:7), GPGGS (SEQ ID NO:11) and GPGGY (SEQ ID NO:7) as amino acid sequence, preferably in this order.

It should be noted that at least two of the repetitive element that is included in the above-mentioned polypeptides silk, are identical to the repeating unit.

Preferably, the silk polypeptide used in the method of the present invention comprises, essentially consists of or consists of:

(i) (GPGXX)n(SEQ ID NO:3) as a repeating element, where X represents any amino acid, preferably in each case independently selected from A, S, G, Y, P, N and Q, and n is 2, 3, 4, 5, 6, 7, 8 or 9;

(ii) (GGX)nas a recurring element, where X represents any amino acid, preferably in each case independently selected from Y, P, R, S, A, T, N and Q, more preferably�individual in each case independently selected from Y, P and Q, and n is 2, 3, 4, 5, 6, 7 or 8; and/or

(iii) (Ax)nas a recurring link, where x is an integer in the range from 5 to 10, and n is 2, 3, 4, 5, 6, 7, 8, 9 or 10.

As mentioned above, at least two repetitive element that is included in the silk polypeptides used in the method of the present invention, are identical to the repeating unit.

Is preferred that the repeating unit were independently selected from module A (SEQ ID NO:20), module C (SEQ ID NO:21), Q (SEQ ID NO:22), the module K (SEQ ID NO:23), module sp (SEQ ID NO:24), module S (SEQ ID NO:25), module R (SEQ ID NO:26), module X (SEQ ID NO:27) or module Y (SEQ ID NO:28) or their variants (that is, the options module And options of module C variants of module Q variants of the module To, variants of the sp module, options of module S, variants of the R, options of module X or options of module Y). Modules A (SEQ ID NO:20) and Q (SEQ ID NO:22) are based on the amino acid sequence of ADF-3 spider Araneus diadematus. Module C (SEQ ID NO:21) basically has the amino acid sequence of ADF-4 spider Araneus diadematus. Modules K (SEQ ID NO:23), sp (SEQ ID NO:24), X (SEQ ID NO:27) and Y (SEQ ID NO:28) are based on the amino acid sequence of the protein FLAG hunting helical thread of the spider Nephila clavipes (WO 2006/008163). Modules S (SEQ ID NO:25) and R (SEQ ID NO:26) are based on resilin (Arthropoda) (WO 2008/155304).

Thus, in one preferred VA�iante the implementation of the present invention, the repeating unit of the silk polypeptide consists of module A: GPYGPGASAAAAAAGGYGPGSGQQ (SEQ ID NO:20), module: GSSAAAAAAAASGPGGYGPENQGPSGPGGYGPGGP (SEQ ID NO:21), Q: GPGQQGPGQQGPGQQGPGQQ (SEQ ID NO:22), module K: GPGGAGGPYGPGGAGGPYGPGGAGGPY (SEQ ID NO:23), module sp: GGTTIIEDLDITIDGADGPITISEELTI (SEQ ID NO:24), module S: PGSSAAAAAAAASGPGQGQGQGQGQGGRPSDTYG (SEQ ID NO:25), module R: SAAAAAAAAGPGGGNGGRPSDTYGAPGGGNGGRPSSSYG (SEQ ID NO:26), module X: GGAGGAGGAGGSGGAGGS (SEQ ID NO:27) or module Y: GPGGAGPGGYGPGGSGPGGYGPGGSGPGGY (SEQ ID NO:28) or their variants.

Preferably, the silk polypeptide used in the method of the present invention comprises, essentially consists of or consists 2-80 repeating units, 3-80 repeating units or 4-60 repeating units, more preferably between 8 to 48 repetitive units, or between 10 to 40 repetitive units and most preferably between 16 to 32 repetitive units, that is, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, 49, 50, 51, 52, 53, 54, 55, 56, 57, 58, 59, 60, 61, 62, 63, 64, 65, 66, 67, 68, 69, 70, 71, 72, 73, 74, 75, 76, 77, 78, 79 or 80 repeating units, which are independently selected from module A (SEQ ID NO:20), module C (SEQ ID NO:21), Q (SEQ ID NO:22), the module K (SEQ ID NO:23), module sp (SEQ ID NO:24), module S (SEQ ID NO:25), module R (SEQ ID NO:26), module X (SEQ ID NO:27) or module Y (SEQ ID NO:28) or their variants (that is, the options module And options of module C variants of module Q variants of module K, variants of the sp module, options of module S, variants of the R, options of module X or options of module Y). It should be noted that at least two repeat�live link, included in the silk polypeptide used in the method of the present invention, are identical to the repeating unit (modules).

Thus, it is preferred that the silk polypeptide used in the method of the present invention, includes, essentially consists of or consists of: (i) duplicate link (links) consisting of module A and/or duplicate link (links), consisting of variants of A module, (ii) duplicate link (links) consisting of module C, and/or duplicate link (links), consisting of variants of the module, (hi) duplicate link (links) consisting of module Q, and/or duplicate link (links), consisting of variants of the module Q, (iv) (a) duplicate link (links) consisting of module A, and a duplicate link (links) consisting of module Q, (b) duplicate link (links) consisting of module A, and a duplicate link (links), consisting of variants of the module Q, (C) duplicate link (links), consisting of variants of module A, and a duplicate link (links) consisting of module Q, (d) repeating link (links), consisting of variants of module A, and a duplicate link (links), consisting of variants of the module Q (v) (a) duplicate link (links) consisting of module A, and a duplicate link (links) consisting of module C, (b) �of Avtoradio link (links), consisting of module A, and a duplicate link (links), consisting of variants of the module, (C) duplicate link (links), consisting of variants of module A, and a duplicate link (links) consisting of module C, (d) duplicate link (links), consisting of variants of module A, and a duplicate link (links), consisting of variants of the module, (vi) (a) duplicate link (links) consisting of module C, and a duplicate link (links), consisting of module Q, (b) duplicate link (links) consisting of module C, and a duplicate link (links), consisting of variants of the module Q, (C) duplicate link (links), consisting of variants of the module, and duplicate link (links) consisting of module Q, (d) duplicate link (links), consisting of variants of the module, and duplicate link (links), consisting of variants of Q, or (vii) (a) duplicate link (links), consisting of module A, the repeating link (links) consisting of module Q, and duplicate link (links) consisting of module C, (b) duplicate link (links) consisting of module A, the repeating link (links) consisting of module Q, and duplicate link (links), consisting of variants of the module, (C) duplicate link (links) consisting of module A, the repeating link (links), consisting of in�options module Q, and duplicate link (links) consisting of module C, (d) duplicate link (links), consisting of variants of module A, the repeating link (links) consisting of module Q, and duplicate link (links) consisting of module C, (e) duplicate link (links) consisting of module A, the repeating link (links), consisting of variants of the module Q, and duplicate link (links), consisting of variants of the module, (f) repeating link (links), consisting of options of module A, the repeating link (links), consisting of variants of the module Q, and duplicate link (links) consisting of module C, (g) repeating link (links), consisting of variants of module A, the repeating link (links) consisting of module Q, and duplicate link (links), consisting of variants of the module, (h) duplicate link (links), consisting of variants of module A, the repeating link (links), consisting of variants of the module Q, and duplicate link (links), consisting of variants of module C.

Modules A, C, Q, K, sp, S, R, X or Y or their versions (i.e. versions of the module A, module options With the options of module Q variants of module K, versions of the sp module, module options S, module options R options of the module or module options Y) can also be combined with each other in any combination and in any quantities� each, that is, the module (redundant link) And can be combined with module (repetitive element) Q (that is, the combination AQ) module (redundant link) can be combined with module (repetitive element) Q (that is, the combination of CQ), the module (redundant link) Q can be combined with module (repetitive element) and a module (redundant link) Q (that is, a combination QAQ), the module (redundant link) And can be combined with module (repetitive element) and a module (redundant link) Q (i.e. a combination AAQ), and so on, provided that the silk polypeptide used in the method of the present invention comprises or consists of at least two repeating units which are identical. For example, the silk polypeptide used in the method of the present invention, may include or be composed of: (An, (AA)n, (AQ)n, (QA)n, Qn, (QQ)n, (QAQ)n, (AQA)n, Cn, (CC)n, (CCC)n, (CQ)n, (QC)n, (QCQ)n, (CQC)n, (AA)nQn, (QQ)nAn, (AAA)nQn, (QQQ)nAn, (AQQ)n, (QQA)n, Knspn, Sn, Rn, Xn, Yn, (Ksp)n, (spK)n, (XY)n, (YX)n, (XX)n, (YY)n, (XXX)n, (YYY)n, (AX)n, (XA)n, (CX)n, (XC)n, (QX)n, (XQ)n, (YQ)n, (QY)n , (SS)n(SR)n, (RS)nor (RR)nwhere n is at least 2, preferably 4, 8, 9, 10, 12, 16, 20, 24 or 32. In the case of the silk polypeptide consisting of (AQ)12, it should be noted that the silk polypeptide module (redundant link) And there are 12 times, and the module (redundant link) Q is also 12 times, and that, thus, the silk polypeptide consists of 24 modules (repeating units). The layout of the units (repeating units) of the silk polypeptide consisting of (AQ)12represents the following: AQAQAQAQAQAQAQAQAQAQAQAQ. In addition, in the case of the silk polypeptide formed from the units (repeating units) of the silk polypeptide consisting of (QAQ)8, it should be noted that the silk polypeptide module (redundant link) And there is 8, and the module (redundant link) Q is present 16 times, and that, thus, the silk polypeptide consists of 24 modules (repeating units). The layout of the units (repeating units) of the silk polypeptide consisting of (QAQ)8represents the following: QAQQAQQAQQAQQAQQAQQAQQAQ.

The silk polypeptide used in the method of the present invention, may also include or consist of the following: (A*Q)n, (AQ*)n, (A*Q*)n, (Q*A)n, (QA*)n, (Q*A*)n, (QAQ*)n, (QA*Q)n, (Q*AQ)n, (QA*Q*)n, (QA*Q) n, (Q*AQ*)n, (Q*A*Q*)n, (AQA*)n, (AQ*A)n(A*QA)n, (AQ*A*)n, (A*Q*A)n(A*QA*)n, (A*Q*A*)nwhere n is, no least 2, preferably 4, 8, 9, 10, 12, 16, 20, 24 or 32, and where * indicates the version of the module, you have the option module A or Q.

The terms "connected" or "linked together" in the context of the present invention may indicate that the modules (repeating unit) combined or linked with each other directly, or in the context of the present invention may indicate that the modules (repeating unit) combined or linked with each other through one or more of the GS spacer amino acids. In preferred embodiments, the modules (repeating unit) included in the silk polypeptide, merged or linked with each other directly. In other preferred embodiments, the modules (repeating unit) included in the silk polypeptide, merged or linked with each other via the GS spacer amino acids in an amount of from 1 to 25 or 1 to 20, more preferably via GS spacer amino acids in an amount of from 1 to 15 or 1 to 10, and most preferably through GS spacer amino acids in an amount of from 1 to 5, that is, through 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24 or 25 GS spacer amino acids. The mentioned Spa�sulfur amino acids can be any amino acid, naturally occurring in proteins. Preferably referred GS spacer amino acid is not Proline. Preferably the GS spacer amino acid (amino acid) having charged groups, independently selected from the group consisting of aspartate, glutamine, histidine and lysine. Mentioned GS spacer amino acids must be amino acids which do not adversely affect the ability of the silk polypeptide to form a coating, it is preferable to form a uniform coating on the inert or naturally occurring material such as Kevlar or wool. In addition, the GS spacer amino acids must be amino acids that do not give rise to steric constraints, such as amino acids, having a small size, such as lysine and cysteine.

In more preferred embodiments, the silk polypeptide comprises modules which are combined with each other directly, and modules, which are combined with each other via the GS spacer amino acids in an amount of from 1 to 25 or 1 to 20, more preferably via GS spacer amino acids in an amount of from 1 to 15 or 1 to 10, and most preferably through GS spacer amino acids in an amount of from 1 to 5, that is, through 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24 or 25 GS spacer amino acids.

p> Option module A, C, Q, K, sp, S, R, X or Y is different from the reference module (wild type) A, C, Q, K, sp, S, R, X or Y, from which he came, until 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14 or 15 amino acid changes in the amino acid sequence (that is, substitutions, accessions, insertions, deletions, the cutoffs from N-Terminus and/or cutoffs with C-end). This version of the module in an alternative or additional embodiment, can be characterized by a certain degree of sequence identity to the reference module (wild type), from which he came. Thus, option module A, C, Q, K, sp, S, R, X or Y is characterized by the identity of the sequence corresponding to the reference module (wild type) A, C, Q, K, sp, S, R, X or Y, component, at least, 50%, 51%, 52%, 53%, 54%, 55%, 56%, 57%, 58%, 59%, 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or even the 99.9%. Preferably, the sequence identity is observed on a continuous stretch of at least 10, 15, 18, 20, 24, 27, 28, 30, 34, 35 or more amino acids, preferably over the entire length of the respective reference module (wild type) A, C, Q, K, sp, S, R, X or Y.

Especially preferred that the sequence identity would be at least 80% over the entire length, would be, at least 85% over the entire length, would be at least 90% over the entire length, would be, at least 95% over the entire length, would be, at least 98% over the entire length, or would be, at least 99% over the entire length of the respective reference module (wild type) A, C, Q, K, sp, S, R, X or Y. in addition, particularly preferred that the sequence identity would be at least 80% on a continuous length, at least in 10, 15, 18, 20, 24, 28 or 30 amino acids, would be, at least 85% on a continuous stretch of at least 10, 15, 18, 20, 24, 28 or 30 amino acids, would be at least 90% on a continuous stretch of at least 10, 15, 18, 20, 24, 28 or 30 amino acids, would be, at least 95% on a continuous length, at least in 10, 15, 18, 20, 24, 28 or 30 amino acids, would be, at least 98% on a continuous stretch of at least 10, 15, 18, 20, 24, 28 or 30 amino acids, or would be, at least 99% in a continuous length, at least 10, 15, 18, 20, 24, 28 or 30 amino acids corresponding to the reference module (wild type) A, C, Q, K, sp, S, R, X or Y.

A fragment (or deletion variant) module A, C, Q, K, sp, S, R, X or Y preferably includes the removal of up to 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14 or 15 amino acids from N-Terminus and/or C-end. The removal can also be internal�.

In addition, variant or fragment of module A, C, Q, K, sp, S, R, X or Y in the context of the present invention is considered to be a variant or a fragment of module A, C, Q, K, sp, S, R, X or Y, only if modifications in relation to the amino acid sequence on which this is based variant or fragment has no negative impact on the ability of the silk polypeptide to form a fiber. Preferably from silk polypeptide comprising a variant or fragment of module A, C, Q, K, sp, S, R, X or Y, it is still possible to extract smooth and uniform fiber at a speed equal to at least 0.1 cm/sec, preferably 10 cm/sec, and more preferably 10 m/sec. A specialist in the relevant field of technology can perform a visual assessment will still be receiving fiber. Smooth and uniform appearance mentioned fiber can be monitored using electron microscopy.

Thus, in one preferred embodiment of the present invention, the repeating unit is independently selected from module AC(SEQ ID NO:29), module AK(SEQ ID NO:30), module CC(SEQ ID NO:31), module WithK1(SEQ ID NO:32), module WithK2(SEQ ID NO:33) or module WithKC(SEQ ID NO:34). Modules AndC(SEQ ID NO: 29), AK(SEQ ID NO:30), CC(SEQ ID NO:31), WITHK1(SEQ ID NO:32)K2(SEQ ID NO:33) and � KC(SEQ ID NO:34) are variants of the module A, which basically has the amino acid sequence of ADF-3 spider Araneus diadematus, and module C, which basically has the amino acid sequence of ADF-4 spider Araneus diadematus, (WO 2007/025719). In the module, AndC(SEQ ID NO:29) the amino acid S (series) at position 21 substituted amino acid (cysteine), in module AK(SEQ ID NO:30) amino acid S at position 21 substituted amino acid K (lysine), in the module WithC(SEQ ID NO:31) the amino acid S at position 25 is substituted for the amino acid, in the module WithK1(SEQ ID NO:32) the amino acid S at position 25 of the substituted amino acid K in the module WithK2(SEQ ID NO:33) an amino acid E (glutamine) at position 20 is substituted with an amino acid K and in the module WithKC(SEQ ID NO:34) an amino acid E at position 20 is substituted with an amino acid K and the amino acid S at position 25 is substituted for the amino acid (WO 2007/025719).

Preferably the repeating unit in the silk polypeptide used in the method of the present invention, comprise the module AndC: GPYGPGASAAAAAAGGYGPGCGQQ (SEQ ID NO:29), module AK:GPYGPGASAAAAAAGGYGPGKGQQ (SEQ ID NO:30), module CC: GSSAAAAAAAASGPGGYGPENQGPCGPGGYGPGGP (SEQ ID NO:31), module WithK1: GSSAAAAAAAASGPGGYGPENQGPKGPGGYGPGGP (SEQ ID NO:32), module WithK2:GSSAAAAAAAASGPGGYGPKNQGPSGPGGYGPGGP (SEQ ID NO:33) or module WithKC: GSSAAAAAAAASGPGGYGPKNQGPCGPGGYGPGGP (SEQ ID NO:34).

Also is preferred that the silk polypeptide used in the method of the present�of the invention, would include, essentially consists of or consists of 2-80 repeating units, 3-80 repeating units or 4-60 repeating units, preferably between 8 to 48 repetitive units, or between 10 to 40 repetitive units and most preferably between 16 to 32 repetitive units, that is, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, 49, 50, 51, 52, 53, 54, 55, 56, 57, 58, 59, 60, 61, 62, 63, 64, 65, 66, 67, 68, 69, 70, 71, 72, 73, 74, 75, 76, 77, 78, 79 or 80 repeating units, which are independently selected from module AC(SEQ ID NO:29), module AK(SEQ ID NO:30), module CC(SEQ ID NO:31), module WithK1(SEQ ID NO:32), module WithK2(SEQ ID NO:33) or module WithKC(SEQ ID NO:34). It should be noted that at least two of the repetitive element that is included in the silk polypeptide used in the method of the present invention, are identical to the repeating unit (modules).

For example, the silk polypeptide used in the method of the present invention, may include or consist of the following: modules WithC4WithC8WithC16WithC32, AC5AndC8or AndC10.

Modules AKWithC, CK1WithK2andKCcan also be combined with each other, that is, the module (redundant link) AKm�can be combined with module (repetitive element) C C(that is, the combination of AKCC), the module (redundant link)K1can be combined with module (repetitive element)K2and with module (repetitive element)KC(that is, the combination of CK1CK2CKCand so on, provided that the silk polypeptide used in the method of the present invention comprises or consists of at least two repeating units which are identical. Thus, the silk polypeptide used in the method of the present invention, may also include or consist of modules (AK)n(WithC)n(WithK1)n(WithK2)n(WithKC)n(AKAndC)n, (CCCC)n, (CK1CK2)n, (CK2CK1)n, (CK1CK2CK1)n, (CK2CK1CK2)n, (CK1CK2CKC)n, (CKCCK2CKC)nor (CCOPCK2CK1)nwhere n is at least 2, preferably 4, 5, 6, 7, 8, 10, 12, 16 or 20. The term "connected" is defined above.

In addition, it is preferred that the silk polypeptide used in the method of the present invention, includes, essentially consists of or consists of: 2-80 repeating units, 3-80 repeating units or 4-60 recurring�HSA links, preferably between 8 to 48 repetitive units, or between 10 to 40 repetitive units and most preferably between 16 to 32 repetitive units, that is, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, 49, 50, 51, 52, 53, 54, 55, 56, 57, 58, 59, 60, 61, 62, 63, 64, 65, 66, 67, 68, 69, 70, 71, 72, 73, 74, 75, 76, 77, 78, 79 or 80 repeating units, which are independently selected from module A (SEQ ID NO:20) or variants thereof, module C (SEQ ID NO:21) or variants thereof, module Q (SEQ ID NO; 22) or variants thereof, module K (SEQ ID NO; 23) or variants thereof, module sp (SEQ ID NO:24) or variants thereof, module S (SEQ ID NO:25) or variants thereof, module R (SEQ ID NO:26) or variants thereof, module X (SEQ ID NO:27) or its variants, module Y (SEQ ID NO:28) or variants thereof, module, AndC(SEQ ID NO:29), module AK(SEQ ID NO:30), module CC(SEQ ID NO:31), module CK1(SEQ ID NO:32), module WithK2(SEQ ID NO:33) or module WithKC(SEQ ID NO:34). Again it should be noted that at least two of the repetitive element that is included in the polypeptide used in the method of the present invention, are identical to the repeating unit (modules).

Modules AndKWithCWithK1WithK2andKCcan also be combined with modules A, C, Q, K, sp, S, R, X or Y, then there is a module (redundant link) AKcan be combined with module (repetitive element) (i.e. a combination sup> K(C), or module (redundant link)Ccan be combined with module (repetitive element) (that is, the combination WithCC) and so on, provided that the silk polypeptide used in the method of the present invention comprises or consists of at least two repeating units which are identical. Thus, the silk polypeptide used in the method of the present invention, may also include, or consist of modules (AQAK)n, (QAK)n, (QAKQ)n(AKQA)n(AKQAK)n, (CCC)n, (CCCC)n, (CCCCC)n, (CCCCC)n, (CCQ)n, (QCC)n, (QCCQ)n, (CWithQC)n, (CQCC)n, (CCQCC)n, (CCK1)n, (CK1C)n, (CK1CC)n, (CCK1C)n, (CKCCKCC)n, (CCKCCKC)n, (CKCQ)n, (QCKC)n, (QCKCQ)n(AKCK1Q)n, (QCK2AK)nor (CKlCK2C)nwhere n is at least. 2, preferably 4, 5, 6, 7, 8, 10, 12, 16 or 20. The term "connected" is defined above.

For example, the silk polypeptide used in the method of the present invention comprises or consists of modules With16 CWithCC16, C8CCC8, C8CC8WithC8C8, C4CC8C4WithC4C8CC4, CC(AQ)24or (AQ)24CC.

The silk polypeptide used in the method of the present invention optionally includes at least one non-repetitive (NR) link, that is, 1, 2, 3, 4, 5, 6 and more links NR, preferably one link NR. In the context of the present invention, the term "non-repetitive (NR) link" relates to the field of amino acids present in the silk polypeptide found in nature, which does not detect any obvious character repetition (unduplicated link or link NR). Preferably the amino acid sequence of non-repeating element corresponds to a non-repetitive amino acid sequence of the polypeptides cord threads found in nature, preferably ADF-3 (SEQ ID NO:1) or ADF-4 (SEQ ID NO:2) or amino acid sequence essentially similar to it.

Especially preferred that the amino acid sequence of non-repeating element would correspond to non-repetitive amino acid sequence of the carboxy-end of frame polypeptides thread found in nature, preferably ADF-3 (SEQ ID NO:1) or ADF-4 (SEQ ID NO:2), Il� amino acid sequence, essentially similar. More preferably, the amino acid sequence of non-repeating element corresponds to a non-repetitive amino acid sequence of the carboxy-end of ADF-3 (SEQ ID NO:1), which includes amino acids from 513 to 636, or ADF-4 (SEQ ID NO:2), which includes amino acids from 302 to 410, or the amino acid sequence essentially similar to them.

In this regard, the term "substantially similar" refers to the degree of amino acid identity, at least for 50%, 51%, 52%, 53%, 54%, 55%, 56%, 57%, 58%, 59%, 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or even 99.9 percent, preferably for 20, 30, 40, 50, 60, 70, 80 or more amino acids, preferably over the entire length, the associated reference non-recurring (carboxy-terminal) amino acid sequence of the polypeptides cord threads found in nature, preferably ADF-3 (SEQ Jo NO:1) or ADF-4 (SEQ ID NO:2).

"Non-recurring" link in the chain comprising the amino acid sequence that is "substantially similar" relevant non-recurring (carboxy-terminal) amino acid sequence in the polypeptide cord threads found in nature (i.e. non-repeating (carboxy-terminal) link wild type), preferably in the range of ADF-3 (SEQ ID NO:1) or ADF-4 (SEQ ID NO:2), so�e is similar in respect to their functional properties, for example, the silk polypeptide comprising the "substantially similar non-recurring link" still has the ability to form a fiber. Preferably from the silk polypeptide comprising the "substantially similar non-recurring link", it is still possible to extract smooth and uniform fiber at a speed equal to at least 0.1 cm/sec, preferably 10 cm/sec, and more preferably 10 m/sec. A specialist in the relevant field of technology can perform a visual assessment will still be receiving fiber. Smooth and uniform appearance mentioned fiber can be monitored using electron microscopy.

Most preferably non-repetitive (NR) link represents a NR3 (SEQ ID NO:41) or a variant thereof, or NR4 (SEQ ID NO:42) or a variant thereof. Link NR3 (SEQ ID NO:41) basically has the amino acid sequence of ADF-3 spider Araneus diadematus, and link NR4 (SEQ ID NO:42) basically has the amino acid sequence of ADF-4 spider Araneus diadematus (WO 2006/008163).

Option link NR3 or NR4 differs from the reference link NR3 (SEQ ID NO:41) or NR4 (SEQ ID NO:42), from which he came, until 1, 2, 3, 4, 5, 6, 7 8 9 10 11, 12, 13, 14, 15, 16, 17. 18, 19, 20, 25 or 30 amino acid changes in the amino acid sequence (that is, substitutions, accessions, insertions, deletions, cutoffs with N-Kansai/or cutoffs with C-end). This version of link NR3 or NR4 in alternative or additional embodiment, can be characterized by a certain degree of sequence identity to the reference link NR3 or NR4, from which he came. Thus, a variant of the link NR3 or NR4 characterized by sequence identity with the corresponding reference link NR3 or NR4, component, at least, 50%, 55%, 60%, 65%, 70%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or even the 99.9%. Preferably, the sequence identity is observed on a continuous stretch of at least 10, 20, 30, 40, 50, 60, 70, 80, 90 or more amino acids, preferably over the entire length of the respective reference level NR3 or NR4.

Especially preferred that the sequence identity would be at least 80% over the entire length, would constitute at least 85% of the entire length, would be at least 90% over the entire length, would be, at least 95% over the entire length, would be, at least 98% over the entire length, or would be, at least 99% over the entire length corresponding to the reference link NR3 or NR4. Furthermore, especially preferred that the sequence identity would be at least 80% on a continuous stretch of at least 20, 30, 40, 50, 60, 70 or 80 amino acids, would be, �about least 85% on a continuous stretch of at least 20, 30, 40, 50, 60, 70 or 80 amino acids, would be at least 90% on a continuous stretch of at least 20, 30, 40, 50, 60, 70 or 80 amino acids, would be, at least 95% on a continuous stretch of at least 20, 30, 40, 50, 60, 70 or 80 amino acids, would be at least 98% on a continuous stretch of at least 20, 30, 40, 50, 60, 70 or 80 amino acids, or would be, at least 99% in a continuous length, at least 20, 30, 40, 50, 60, 70 or 80 amino acids corresponding to the reference link NR3 or NR4.

A fragment (or deletion variant) link NR3 or NR4 preferably includes the removal of up to 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 30, 35, 40, 45, 50, 55 or 60 amino acids from N-Terminus and/or C-end. The removal can also be internal.

In addition, a variant or a fragment link NR3 or NR4 in the context of the present invention is considered to be a variant or a fragment link NR3 or NR4, only if modifications in relation to the amino acid sequence on which this is based variant or fragment has no negative impact on the ability of the silk polypeptide to form a fiber. Preferably from silk polypeptide comprising a variant or fragment link NR3 or NR4, it is still possible to extract g�alcoho and homogeneous fiber at a speed, component of at least 0.1 cm/sec, preferably 10 cm/s 20 cm/s 50 cm/sec, 75 cm/h, 1 m/sec, 2 m/h, 3 km/h, 4 km/h, 5 km/h, and more preferably 10 m/sec. A specialist in the relevant field of technology can perform a visual assessment will still be receiving fiber. Smooth and uniform appearance mentioned fiber can be monitored using electron microscopy.

In an alternative embodiment, can be tested against whether the variant or fragment link NR3 or NR4 still to secure the passage of polymerization and/or increase the solubility of the polypeptide silk in which it is included. Specialist in the art can easily evaluate whether the silk polypeptide comprising a variant or fragment link NR3 or NR4, possess the above-mentioned functional properties similar to the properties of the silk polypeptide that includes appropriate reference link NR3 or NR4. Suitable for use assays well known to those skilled in the art. For example, polymerization of silk polypeptides comprising a variant or fragment link NR3 or NR4, and polymerization for silk polypeptides, including appropriate reference link NR3 or NR4, can be easily visualized when using native �spruce electrophoresis. The solubility of the silk polypeptide comprising a variant or fragment link NR3 or NR4, and the solubility of the silk polypeptide that includes appropriate reference link NR3 or NR4, can be subjected to a simple test as a result of saturation mentioned polypeptides silk aqueous solution. The results, in conclusion, it can be matched with each other.

Preferably, the silk polypeptide used in the method of the present invention, is selected from the group consisting of ADF-3 (SEQ ID NO:1) or variants thereof, ADF-4 (SEQ ID NO:2) or variants thereof, MaSp I (SEQ ID NO:43) or variants thereof, MaSp II (SEQ ID NO:44) or its variants, (C)m, CnNRz, NRz(C)m, (AQ)n, (AQ)nNRz, NRz(AQ)n, (QAQ)o, NRz(QAQ)o, (QAQ)oNRz, Yp, Xpand KPwhere m is an integer in the range from 8 to 48 (that is, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47 or 48), n is an integer in the range from 4 to 24 (that is, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15. 16, 17, 18, 19, 20, 21, 22, 23 or 24), o is an integer in the range from 2 to 20 (that is, 2, 3,4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19 or 20), p is an integer in the range from 8 to 16 (that is, 8, 9, 10, 11, 12, 13, 14, 15 or 16), a z is an integer in the range from 1 to 3 (that is 1, 2 or 3), preferred�flax 1, a NR stands for non-recurring link. The above formula is defined by one of the following next: in the formula

(i) (C)m- combined with each other, the number "m" of modules, namely from 8 to 48 modules, introducing amino acid sequence corresponding to SEQ ID NO:21,

(ii) (C)mNRz- combined with each other, the number "m" of modules, namely from 8 to 48 modules, introducing amino acid sequence corresponding to SEQ ID NO:21, where the mentioned modules With additionally combined with the number "z" non-repetitive (NR) units, namely non-repetitive (NR) units in amounts in the range from 1 to 3, for example with non-repetitive (NR) units NR3 represented amino acid sequence corresponding to SEQ ID NO:41 or NR4 represented amino acid sequence corresponding to SEQ ID NO:42,

(iii) NRz(C)m- is present (z=1) or combined with each other (z=2 or 3) number of "z" non-repetitive (NR) units, namely 1 to 3 non-repetitive (NR) units, e.g. non-repetitive (NR) units NR3 represented amino acid sequence corresponding to SEQ ID NO:41 or NR4 represented amino acid sequence corresponding to SEQ ID NO:42, which referred to non-repetitive (NR) link (link) is additionally combined with the number "m" �of Tula With, namely modules, introducing amino acid sequence corresponding to SEQ ID NO:21, in an amount in the range from 8 to 48,

(iv) (AQ)n- combined with each other, the number "n" combinations of modules A and Q, namely from 6 to 24 combinations of modules A and Q, where module a is amino acid sequence corresponding to SEQ ID NO:20, and the module Q is amino acid sequence corresponding to SEQ ID NO:22,

(v) (AQ)nNRz- combined with each other, the number "n" combinations of modules A and Q, namely from 6 to 24 combinations of modules A and Q, where module a is amino acid sequence corresponding to SEQ ID NO:20, and the module Q is amino acid sequence corresponding to SEQ ID NO:22, and where the said combination of modules A and Q optionally combined with the number "z" non-repetitive (NR) units, namely non-repetitive (NR) units in amounts in the range from 1 to 3, for example with non-repetitive (NR) the units NR3 represented amino acid sequence corresponding to SEQ ID NO:41 or NR4 represented amino acid sequence corresponding to SEQ ID NO:42,

(vi) NRz(AQ)n- is present (z=1) or combined with each other (z=2 or 3) number of "z" non-repetitive (NR) units, namely 1 to 3 non-repetitive (NR) units, e.g. �autoresize (NR) units NR3, introducing the amino-acid sequence corresponding to SEQ ID NO:41 or NR4 represented amino acid sequence corresponding to SEQ ID NO:42, which referred to non-repetitive (NR) link (link) is additionally combined with the number "n" combinations of modules A and Q, namely the combinations of modules A and Q in amounts in the range of 6 to 24, where the module And represents the amino acid sequence corresponding to SEQ ID NO:20, and the module Q is amino acid sequence corresponding to SEQ ID NO:22,

(vii) (QAQ)o- combined with each other, the number of "on" combinations of modules Q, A and Q, namely 8 to 16 combinations of modules Q, A and Q, where Q represents the amino acid sequence corresponding to SEQ ID NO:22, and the module And represents the amino acid sequence corresponding to SEQ ID NO:20,

(viii) (QAQ)oNRz- combined with each other, the number of "on" combinations of modules Q, A and Q, namely 8 to 16 combinations of modules Q, A and Q, where Q represents the amino acid sequence corresponding to SEQ ID NO:22, and the module And represents the amino acid sequence corresponding to SEQ ID NO:20, and where the said combination of modules Q, and Q optionally combined with the number "z" non-repetitive (NR) units, namely non-repetitive (NR) the links in the quantity range of�not from 1 to 3, for example with non-repetitive (NR) units NR3 represented amino acid sequence corresponding to SEQ ID NO:41 or NR4 represented amino acid sequence corresponding to SEQ ID NO:42,

(ix) NRz(QAQ)o - is present (z=1) or combined with each other (z=2 or 3) number of "z" non-repetitive (NR) units, namely 1 to 3 non-repetitive (NR) units, e.g. non-repetitive (NR) units NR3 represented amino acid sequence corresponding to SEQ ID NO:41 or NR4 represented amino acid sequence corresponding to SEQ ID NO:42, which referred to non-repetitive (NR) link (link) is additionally combined with the number of "on" combinations of modules Q, A and Q, namely the combinations of modules Q, A and Q in amounts in the range from 8 to 16, where Q represents the amino acid sequence corresponding to SEQ ID NO:22, and the module And represents the amino acid sequence corresponding to SEQ ID NO:20,

(x) Yp- combined with each other, the number "p" modules Y, namely 8 to 16 modules Y submitted amino acid sequence corresponding to SEQ ID NO:28,

(xi) Xp- combined with each other, the number "p" of modules X, namely 8 to 16 modules X, introducing amino acid sequence corresponding to SEQ ID NO:27, and

(xii) Kp- United �Rog other number "p" of modules K, namely 8 to 16 modules K, introducing amino acid sequence corresponding to SEQ ID N0:23.

More preferably

(i) z (C)mNRzor NRz(C)mis 1, m represents a whole number in the range from 8 to 48 (that is, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33,34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47 or 48), z in (C)mNRzor NRz(C)mis 2, m represents a whole number in the range from 8 to 48 (that is, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47 or 48) or z (C)mNRzor NRz(C)mis 3, and m represents an integer in the range from 8 to 48 (that is, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47 or 48),

(ii) z (AQ)nNRzor NRz(AQ)nis 1, and n is an integer in the range from 4 to 24 (that is, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23 or 24), z (AQ)nNRzor NRz(AQ)nis 2, a n is an integer in the range from 4 to 24 (that is, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23 or 24) or z (AQ)nNRzor NRz(AQ)nis 3, and n is an integer in the range from 4 to 24 (that is, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23 or 24),

(iii) z NRz(QAQ) oor (QAQ)oNRzis 1 and o is an integer in the range from 2 to 20 (that is, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19 or 20), z NRz(QAQ)oor (QAQ)oNRzis 2 and o is an integer in the range from 2 to 20 (that is, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19 or 20) or z NRz(QAQ)oor (QAQ)oNRzis 3 and o is an integer in the range from 2 to 20 (that is, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19 or 20),

where NR denotes a non-repeating element, preferably NR3 or NR4.

Most preferably, the silk polypeptide used in the method of the present invention, represents a C16NR3, C32NR3, C16NR4, C32NR4, (AQ)12, (AQ)24, (AQ)12NR3, (AQ)24NR3, (AQ)12NR4, (AQ)24NR4, C16, C32, Y8, Y16, X8, X16, K8or K16.

Option ADF-3, ADF-4, MaSp I or MaSp II differs from a reference polypeptide (wild type) ADF-3 (SEQ ID NO:1), ADF-4 (SEQ ID NO:2), MaSp I (SEQ ID NO:43) or MaSp II (SEQ ID NO:44), from which he came, up to 150 (up to 1,2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 25, 30, 35,40,45, 50, 55, 60, 65, 70, 75, 80, 85, 90, 95, 100, 110, 120, 130, 140 or 150) amino acid changes in the amino acid sequence (that is, substitutions, accessions, insertions, deletions, clippings from N-Terminus and/or cutoffs from p-�of once). Such an option in alternative or additional embodiment, can be characterized by a certain degree of sequence identity to a reference polypeptide (wild type), from which he came. Thus, a variant of ADF-3, ADF-4, MaSp I or MaSp II is characterized by the sequence identity with the corresponding reference polypeptide (wild type) ADF-3, ADF-4, MaSp I or MaSp II, component, at least, 50%, 51%, 52%, 53%, 54%, 55%, 56%, 57%, 58%, 59%, 60%, 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or even the 99.9%. Preferably, the sequence identity is observed on a continuous stretch of at least 20, 25, 30, 35, 40, 50, 60, 70, 80, 90, 100, 120, 150, 180, 200, 250, 300, 350, 400 or more amino acids, preferably over the entire length of the respective reference polypeptide (wild type) ADF-3, ADF-4, MaSp I or MaSp II.

Especially preferred that the sequence identity would be at least 80% over the entire length, would constitute at least 85% of the entire length, would be at least 90% over the entire length, would be, at least 95% over the entire length, would be, at least 98% over the entire length, or would be, at least 99% over the entire length corresponding to the reference polypeptide (wild type) ADF-3, ADF-4, MaSp I or MaSp II. In addition, especially before�chitaetsa, to the identity of the sequence would be, at least 80% on a continuous stretch of at least 20, 30, 50, 100, 150, 200, 250 or 300 amino acids, would be, at least 85% on a continuous stretch of at least 20, 30, 50, 100, 150, 200, 250 or 300 amino acids, would be at least 90% on a continuous stretch of at least 20, 30, 50, 100, 150, 200, 250 or 300 amino acids, would be, at least 95% on a continuous stretch of at least 20, 30, 50, 100, 150, 200, 250 or 300 amino acids, would be, at least 98% on a continuous stretch of at least 20, 30, 50, 100, 150, 200, 250 or 300 amino acids, or would be, at least 99% in a continuous length, at least 20, 30, 50, 100, 150, 200, 250 or 300 amino acids corresponding to the reference polypeptide (wild type) ADF-3, ADF-4, MaSp I or MaSp II.

A fragment (or deletion variant) polypeptide ADF-3 (SEQ ID NO:1) preferably includes the removal of up to 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 15, 20, 25, 30, 35, 40, 45, 50, 55, 60, 65, 70, 75, 80, 85, 90, 95, 100, 120, 150, 170, 200, 220, 250, 270, 300, 320, 350, 370, 400, 420, 450, 470, 500, 520, 550, 570, 600 or 610 amino acids from N-Terminus and/or C-end. The removal can also be internal.

A fragment (or deletion variant) polypeptide ADF-4 (SEQ ID NO:2) preferably includes the removal of up to 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 15, 20, 25, 30, 35, 40, 45, 50, 55, 60, 65, 70,75, 80, 85, 90, 95, 100, 120, 150, 170, 200, 220, 250, 270, 30, 320, 330, 340, 350, 360, 370, 380 or 390 amino acids from N-Terminus and/or C-end. The removal can also be internal.

A fragment (or deletion variant) polypeptide MaSp I (SEQ ID NO:43) preferably includes the removal of up to 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 15, 20, 25, 30, 35, 40, 45, 50, 55, 60, 65, 70, 75, 80, 85, 90, 95, 100, 150, 200, 250, 300, 350, 400, 450, 500, 550, 600, 620, 640, 660, 670, 680 or 690 amino acids from N-Terminus and/or C-end. The removal can also be internal.

A fragment (or deletion variant) polypeptide MaSp II (SEQ ID NO:44) preferably includes the removal of up to 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 15, 20, 25, 30, 35, 40, 45, 50, 55, 60, 65, 70, 75, 80, 85, 90, 95, 100, 150, 200, 250, 300, 350, 400, 450, 500, 520, 540, 560 or 570 amino acids from N-Terminus and/or C-end. The removal can also be internal.

In addition, variant or fragment of ADF-3, ADF-4, MaSp I or MaSp II in the context of the present invention is considered to be a variant or fragment of ADF-3, ADF-4, MaSp I or MaSp II only if modifications in relation to the amino acid sequence on which this is based variant or fragment has no negative impact on the ability of the silk polypeptide to form a fiber. Preferably from silk polypeptide comprising a variant or fragment of ADF-3, ADF-4, MaSp I or MaSp II, it is still possible to extract smooth and uniform fiber at a speed equal to at least 0.1 cm/sec, preferably 10 cm/sec, and more preferably 10 m/sec. With�ecialist in the art can perform a visual assessment of will there still be a receiving fiber. Smooth and uniform appearance mentioned fiber can be monitored using electron microscopy.

Preferably, the method is implemented at temperatures in the range from 5°C to 60°C, more preferably at temperatures in the range from 10°C to 50°C, and most preferably at temperatures in the range from 20°C to 40°C. Thus, the method can be implemented at a temperature of 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, 49, 50, 51, 52, 53, 54, 55, 56, 57, 58, 59 or 60°C.

Preferably, the method is implemented at a pressure in the range from 10 kPa to 1000 kPa, more preferably from 40 kPa to 500 kPa, and most preferably from 50 kPa to 150 kPa. Thus, the method can be implemented with 10, 20, 30, 40, 50, 60, 70, 80, 90, 100, 150, 200, 250, 300, 350, 400, 450, 500, 550, 600, 650, 700, 750, 800, 950, 1000 kPa. Particularly preferred that the method would be implemented in standard conditions for temperature and pressure, i.e. at 20°C and 101.325 kPa.

In preferred embodiments of the present invention, the spinning solution obtained in stage (a) contains more than one polymer, preferably 2, 3 or 4 of the polymer, for example a polypeptide, such as silk polypeptides, casein, Zein, or BSA. For example, the spinning solution obtained in stage (a), mo�em to contain (i) the polypeptide of silk and casein, (ii) the polypeptide of silk and Zein, (iii) the polypeptide of silk and BSA, (iv) the polypeptide of silk, Zein and casein, (v) a polypeptide silk, casein and BSA, (vi) a polypeptide silk, BSA, casein and Zein, (vi) Zein and casein, (viii) Zein and BSA, (ix) casein and BSA or (x) Zein and casein and BSA. The polypeptides can be labeled, for example, enzyme labels, Biotin, radioactive or fluorescent labels, such as fluorescein (FITZ).

In other preferred embodiments of the present invention, the spinning solution obtained in stage (a) contains more than one type of polypeptide silk. Preferably, the spinning solution obtained in stage (a) of the method of the present invention, contains 2, 3, 4, 5, 6, 7, 8, 9 or 10 different types of silk polypeptides, most preferably 2 different types of silk polypeptides. For example, the spinning solution may contain polypeptides spider silk cord threads, which differ from each other in respect to their amino acid sequence. Spinning carried out in the method of the present invention, may also include polypeptides spider silk cord threads and silk trailing spiral thread of a spider, which differ from each other in respect of their natural origin. The polypeptide of spider silk cord threads occurs in a large inuloides gland, while the polypeptide hunting spiral �ichi occurs in zhutkovatoy (flagelliform) gland.

The concentration of the polymer, for example, the silk polypeptide, BSA, Zein or casein, is preferably in the range from 0.15 mg/ml to 500 mg/ml, more preferably in the range from 0.15 mg/ml up to 99.9 mg/ml, in the range from 0.15 mg/ml to 90 mg/ml, in the range from 0.15 mg/ml to 80 mg/ml, in the range from 0.15 mg/ml to 70 mg/ml, in the range of 0.15 mg/ml to 60 mg/ml or in the range from 0.15 mg/ml to 50 mg/ml, most preferably in the range from 0.5 mg/ml to 50 mg/ml, 0.5 mg/ml to 40 mg/ml, 0.5 mg/ml to 30 mg/ml or in the range of 1 mg/ml to 20 mg/ml. especially preferred that the concentration of the polymer, for example, the silk polypeptide, BSA, Zein or casein, would be in the range from 0.15 mg/ml to 20 mg/ml.

Thus, for example, the concentration of the polymer, for example the polypeptide of silk, casein, Zein, or BSA, is at least 0.15 mg/ml, 0.2 mg/ml, 0.3 mg/ml, 0.4 mg/ml, 0.5 mg/ml, 0.6 mg/ml, 0.7 mg/ml, 0.8 mg/ml, 0.9 mg/ml, 1 mg/ml, 2 mg/ml, 3 mg/ml, 4 mg/ml, 5 mg/ml, 6 mg/ml, 7 mg/ml, 8 mg/ml, 9 mg/ml, 10 mg/ml, 11 mg/ml, 12 mg/ml, 13 mg/ml, 14 mg/ml, 15 mg/ml, 16 mg/ml, 17 mg/ml, 18 mg/ml, 19 mg/ml, 20 mg/ml, 21 mg/ml, 22 mg/ml, 23 mg/ml, 24 mg/ml, 25 mg/ml, 26 mg/ml, 27 mg/ml, 28 mg/ml, 29 mg/ml, 30 mg/ml, 31 mg/ml, 32 mg/ml, 33 mg/ml 34 mg/ml, 35 mg/ml 36 mg/ml, 37 mg/ml 38 mg/ml, 39 mg/ml, 40 mg/ml, 41 mg/ml, 42 mg/ml, 43 mg/ml, 44 mg/ml, 45 mg/ml, 46 mg/ml, 47 mg/ml, 48 mg/ml, 49 mg/ml, 50 mg/ml, 55 mg/ml, 60 mg/ml, 65 mg/ml, 70 mg/ml, 75 mg/ml, 80 mgml, 85 mg/ml, 90 mg/ml 95 mg/ml, 100 mg/ml, 110 mg/ml, 120 mg/ml, 130 mg/ml, 140 mg/ml, 150 mg/ml, 160 mg/ml, 170 mg/ml, 180 mg/ml, 190 mg/ml, 195 mg/ml, 200 mg/ml, 250 mg/ml, 300 mg/ml or 350 mg/ml.

It should be noted that the method of the present invention requires only very low concentrations of polymers, such as silk polypeptides, ranging from concentrations constituting only 0.15 mg/ml, and preferably to concentrations not greater than 90 mg/ml, more preferably not larger than 50 mg/ml, and most preferably not greater than 20 mg/ml. the Advantage of this lies in the very low shear viscosity of the spinning solution used in the method of the present invention that, in turn, improves the processability mentioned spinning solution.

A compound that increases the viscosity, by its structure, no restrictions are applied as long as it will increase the longitudinal viscosity of the spinning solution.

Preferably, the compound that increases the elongation viscosity of the solution is a linear or branched polymer having a molecular weight equal to at least 20 kDa, for example of 25 kDa, 30 kDa, 40 kDa, 50 kDa, 60 kDa, 70 kDa, 80 kDa, 90 kDa, 100 kDa, 200 kDa, 300 kDa, 400 kDa, 500 kDa, 600 kDa, 700 kDa, 800 kDa and 900 kDa to 1 MDA, 1.5 MDA 2 MDA, 2.5 MDA 3 MDA, 3,5 Hmm, 4 Hmm, 4,5 Hmm Il� 5 MDA. Is preferred to a linear or branched polymer had a molecular weight ranging from 20 kDa to 5 MDA or from 50 kDa to 4 MDA, more preferably from 100 kDa to 2 MDA or from 100 kDa to 1 MDA.

More preferably, the compound that increases the elongation viscosity of the solution is a linear or branched polymer having a molecular weight equal to at least 500 kDa, for example of 550 kDa, 600 kDa, 650 kDa, 700 kDa, 750 kDa, 800 kDa, 850 kDa to 900 kDa, 950 kDa to 1 MDA, 1.5 MDA 2 MDA, 2.5 MDA 3 MDA, 3.5 MDA 4 MDA, 4,5 MDA or 5 MDA. More is preferred to a linear or branched polymer had a molecular weight in the range from 500 kDa to 5 MDA or 900 kDa to 5 MDA, most preferably from 1 to 4 MDA MDA or 1 MDA 3 MDA.

Is preferred that the compound which increases the longitudinal viscosity of the fluid, would be selected from the group consisting of polyacrylamide (PAA), polyethylene (PE), polyethylene glycol (PEG), polysaccharides, dekstranov, polyvinyl alcohols, nucleic acids and their mixtures. In one preferred embodiment of the dextran is a dextran-sulfate.

Preferably, the compound that increases the elongation viscosity of the solution is a polyethylene glycol (PEG) having a molecular weight equal to at least 20 kDa, for example 25 to�and, 30 kDa, 40 kDa, 50 kDa, 60 kDa, 70 kDa, 80 kDa, 90 kDa, 100 kDa, 200 kDa, 300 kDa, 400 kDa, 500 kDa, 600 kDa, 700 kDa, 800 kDa and 900 kDa to 1 MDA, 1.5 MDA 2 MDA, 2.5 MDA 3 MDA, 3.5 MDA 4 MDA, 4,5 MDA or 5 MDA. Is preferred that the polyethylene glycol (PEG) having a molecular weight ranging from 20 kDa to 5 MDA or from 50 kDa to 4 MDA, more preferably from 100 kDa to 2 MDA or from 100 kDa to 1 MDA.

More preferably, the compound that increases the elongation viscosity of the solution is a polyethylene glycol (PEG) having a molecular weight equal to at least 500 kDa, for example of 550 kDa, 600 kDa, 650 kDa, 700 kDa, 750 kDa, 800 kDa, 850 kDa to 900 kDa, 950 kDa to 1 MDA, 1.5 MDA 2 MDA, 2.5 MDA 3 MDA, 3.5 MDA 4 MDA, 4,5 MDA or 5 MDA. A more preferred that the polyethylene glycol (PEG) having a molecular weight in the range from 500 kDa to 5 MDA or 900 kDa to 5 MDA, most preferably from 1 to 4 MDA MDA or 1 MDA 3 MDA.

The concentration of compound that increases the elongation viscosity of the solution is preferably in the range from 0.1% (wt./about.) up to 5% (wt./vol.), more preferably in the range from 0.5% (wt./about.) up to 4% (wt./vol.), and most preferably in the range from 1% (wt./about.) up to 3% (wt./vol.).

Thus, for example, the concentration of compound that increases the elongation viscosity of the solution is 0,1, 0,2, 0,3, 0,4, 0,5, 0,6, 0,7, 0,8, 0,9, 1,0, 1,1, 1,2, 1,3, 1,4, 1,5, 1,6, 1,7, 1,8, 1,9, 2,0 2,1, 2,2, 2,3, 2,4, 2,5, 2,6, 2,7, 2,8, 2,9, 3,0, 3,1, 3,2, 3,3, 3,4, 3,5, 3,6, 3,7, 3,8, 3,9, 4,0, 4,1, 4,2, 4,3, 4,4, 4,5, 4,6, 4,7, 4,8, 4,9 or 5% (wt./vol.).

As, to his surprise, found the inventors of the present invention, this already low concentration of compound that increases the elongation viscosity of the solution is sufficient for spinning fibers when using the method proposed in this paper. Low concentration mentioned compounds, on the one hand, longitudinal increases the viscosity of the solution, but, on the other hand, essentially increases the shear viscosity of the solution, so that the formation of fibers is improved. Thus, the spinning solution used in the method of the present invention is mainly formed of a polymer such as a polypeptide silk, Zein or casein, i.e. it is relatively clean. Furthermore, due to the moderate use of compounds or substances in addition to the polymer, such as a polypeptide silk, Zein or casein, the method of the present invention is economical cost and environmentally safe.

The ratio of the values % (mass.) between the silk polypeptide and improver of the longitudinal viscosity is preferably in the range from 0.1 to 5 from 0.2 to 5, from 0.3 to 5, or from 0.4 to 5, more preferably from 0.4 to 2, most preferably from 0.8 to 1.5. Thus, in the preferred�'s implementation options, in which the silk polypeptide is present in the solution in an amount in the range of 1 to 20 mg/ml, the number improver longitudinal viscosity is selected so that the ratio of the values % (mass.) between the silk polypeptide and improver of the longitudinal viscosity is preferably in the range from 0.1 to 10, more preferably from 0.2 to 5, more preferably from 0.4 to 2, most preferably from 0.8 to 1.5.

For example, the addition of high molecular weight polyacrylamide (5 MDA,1% (wt./about.)) the number ohnesorg the C16the spinning solution may be increased sufficiently to provide an improved receiving fiber on the interfacial surface of the air/liquid.

The solvent can be any solution in which soluble polymer, for example a polypeptide such as a polypeptide of spider silk, Zein, BSA or casein, and a polymer that improves the longitudinal viscosity. Is preferred that the solvent be selected from the group consisting of a polar solvent, preferably water, aqueous buffer, alcohol, preferably isopropanol, hexafluoroisopropanol, glycerol, ethanol (EUN), propanol, butanol, octanol or acetone; non-polar solvent, preferably hexane, dodecane or oils, other organic solvents, preferably ethyl acetate; and mixtures thereof. �thus, the solvent may also be a mixture of a polar solvent, such as water, and a nonpolar solvent such as hexane. In one preferred embodiment of the pH value of the solvent is in the range from 4 to 10.

It should be noted that due to the combined use of very low concentrations of polymers, such as polypeptides silk, Zein or casein, and very low concentrations of compounds that increase the elongation viscosity of the solution u of the spinning solution, when using the method of the present invention may be facilitated obtaining fiber.

In addition, due to the combined use of very low concentrations of polymers, such as polypeptides silk, Zein or casein, and very low concentrations of compounds that increase the elongation viscosity of the solution u of the spinning solution, the said solution has a high viscosity consistency, in contrast to other spinning solutions of the prior art. Thereby can be improved processability of the spinning solution.

Preferably fiber hood initiate the introduction of interfacial surface air/liquid or liquid/liquid in the solution in contact with the tool for extraction and removal tool for drawing monsters from�NLRB interfacial surface. The term "air" in accordance with the use herein preferably refers to a mixture of gases occurring naturally in the earth's atmosphere. In the context of interfacial surface liquid/liquid, where one of the fluids is a spinning solution, is preferred to another fluid would be poorly miscible with the spinning solution. Accordingly, in the case of the solvent of the spinning solution in the form of a polar solvent other liquid would preferably be non-polar. Alternatively, in the case of the solvent of the spinning solution in the form of a non-polar solvent preferably other liquid will be polar. The interface liquid/fluid can also be obtained, at least temporarily, when administered in contact with each other of two miscible liquids, for example, in the pipe, where one liquid stream covers the flow of the second liquid. As you can imagine no desire to tie himself to any theory, the initial introduction of the interfacial surface in contact with the tool for drawing, such as a pipette tip, creates for polymers in the spinning solution attachment point. The withdrawal of the pipette leads to the orientation of the polymers in the solvent turning their head or tail to the tool for extraction, resulting in polymers expressed�stabilize side-by-side with each other, and increasingly associated with each other. Upon subsequent withdrawal of the polymers move from ordered States relating to the type of solution or liquid crystal, semi-solid or solid state. The term "hood" in this context is used to refer only to initiate this process of alignment, but also to denote continuous drain aligned or partially aligned polymer molecules from the spinning solution. During this condition, preferably continuous extrude tool to extrude no longer is in contact with the spinning solution, but produces a "hood" further polymer molecules from the solution in the separated solution, i.e. a solution containing aligned polymers, no longer in contact with the main mass of the spinning solution. Thus, in the context of the present invention, the term "extract" refers to the hood as the process of obtaining fiber, which can also include stretching or hardening. In addition, drawing fiber from a solution is not a process limited by pulling the fibers separated from the solution in the use of tools for drawing, such, for example, a glass needle, as shown in example 1. The method can also include any appropriate automated system, such as a pipe through which the Rast�PR taken away at compensating for, with the nozzle on the end where the spinning solution is extruded and taken a tool for drawing, thereby conducts continuous fiber hood extruded spinning solution. Tool for drawing can be any type of tool with a tip, the respective fiber hood and made of a suitable material, for example, can provide the point of attachment to the polymer in the spinning solution. Examples include the following, but are not limited to only these: pipette tips, needles or thin rods made of plastic, metal or glass. The speed fiber hoods are no restrictions do not impose up until it is high enough to extrude a thin fluid elementary fiber that will exist for a sufficiently long period of time to ensure evaporation of the solvent and obtain a fiber, preferably a thin, lightweight and long fibers. However, in one preferred embodiment of the extraction is carried out as a result of contact of the solution with the tool for drawing and works drawing fiber from the surface. During the operation, that is, upon receipt of the initial contact surface and the extraction of fibers from the surface, the term "hood" also� refers to the removal of fibers from the solution, preferably at a constant speed. The ideal speed depends on the viscosity of the spinning solution, i.e. on the type and concentration of polymers used, and must be defined in the experiment. Preferably the extraction is carried out at speeds comprising at least 0.1 cm/sec, preferably in the range from 0.1 cm/sec to 15 m/sec 1 cm/sec to 5 m/sec, from 3 cm/sec to 1 m/sec 5 cm/sec to 50 cm/sec 5 cm/s to 15 cm/sec, and more preferably of 10 cm/sec. For example, extraction is carried out at speeds comprising at least, 0,1, 0,5, 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 20, 30, 40, 50, 60, 70, 80, 90 cm/sec, 1, 1,5, 2, 2,5, 3, 3,5, 4, 4,5, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14 or 15 km/h.

In the method of the invention also provides for the extrusion of the spinning solution to obtain fiber. The term "extrusion" in this context means an Annex to the spinning solution pressure for forcing it through the hole, such as a nozzle. In the field of polymer technology ways of "extrusion" is often used to produce fibers from molten thermoplastics, i.e. the total extruded material hardens after leaving the holes. In the context of the present invention, the extruded spinning solution is not completely solidified. Instead, the dissolved polymers that content�tsya in extruded spinning solution, associated with the formation of the fiber, which is usually smaller in diameter than the hole through which the spinning solution is extruded, while separating from the thus obtained fiber residual solvent. In one preferred embodiment of the originally obtained fiber is attached to the device extraction of the fiber, for example a cylinder, spool or reel on which the fiber is continuously wound. Depending on the relative speed of the cylinder relative to the speed of obtaining the fiber during the extrusion may also occur and pull forces acting on the extruded fiber, the fiber in some embodiments, may be considered subject to "extract" from the extruded solution.

For additional improvement in predmosti spinning solution simultaneously with the longitudinal viscosity can be increased and the shear viscosity spinning artificial syrups to a value that does not harm the processing fluid, for example, by addition of improvers Newtonian viscosity. Thus, predmosti indicates the suitability of the spinning solution for fiber hoods.

Thus, in one embodiment the spinning solution further comprises connected�e, that increases the Newtonian viscosity, preferably monosaccharides, such as glucose, galactose or fructose; disaccharides, such as lactose or sucrose; polysaccharides, such as glycogen; or polyols, for example, Inositol, sorbitol, glycerol or polyglycols; or mixtures thereof.

Preferably, the spinning solution further comprises dispersed therein particulate material. Upon receipt of this fiber particulate material of relatively uniform manner is embedded in the fiber. The dispersed material in his compositions, no restrictions are applied until such time as it will be suitable for use when included in the fiber. Is preferred to disperse the material would be selected from the group consisting of granules, metals that conduct electricity (including gold, copper), crystallites of protein complexes/protein, enzymes (for example, green fluorescent protein (SFB) or β-galactosidase) and cells (for example, osteoblasts human cells or precursor cells of tendons person or any pluripotent cells or stem cells). Preferably the cells are selected from cells, secreting enzymes or hormones, such as islet cells of Langerhans. The preferred crystallites are dyes that are insoluble in water, fluorescent dyes (eg�emer, stanovy red) or azo dyes (for example, Nile red).

On the concentration of particulate material in the spinning solution, no restrictions are applied. Preferably the dispersed material in the spinning solution is present in amounts in the range from 0.01% (wt./about.) up to 10% (wt./vol.), preferably from 0.5% (wt./about.) up to 1% (wt./vol.). Thus, the dispersed material in the spinning solution may be present in the amount of 0,01, 0,05, 0,1, 02, 0,3, 0,4, 0,5, 0,6, 0,7, 0,8, 0,9, 1,0, 1,5, 2,0, 2,5, 3,0, 3,5, 4,0, 4,5, 5,0, 5,5, 6,0, 6,5, 7,0, 7,5. 8,0, 8,5, 9,0, 9,5, 10,0% (mass./vol.).

In one preferred embodiment the spinning solution further comprises a compound that increases the Newtonian viscosity, for example polyglycols, or particulate material, such as pellets. In yet another preferred embodiment of the spinning solution further contains a compound that increases the Newtonian viscosity, for example polyglycols and particulate material, for example, granules.

The fiber after the receipt can be treated as a result of curing in a curing solution or stitching. Thus, it is preferred that the method of the present invention, after step (b) includes a stage (C) curing the fiber in a curing solution or staple fiber.

Crosslinking may include�AMB connection other connections with fiber or connection identical or different fibers with each other, in the result that can be obtained, for example, a multi-fiber structures, such as multilayer fiber, or structure "core-shell".

The term "crosslinking" in accordance with the usage in this document relates to a method of a chemical compound of two molecules by a covalent bond. Crosslinking reagents or reaction combinations are end groups, reactive in relation to specific functional groups (primary amines, sulfhydryl and the like) polypeptides or other molecules. Preferably, the crosslinking reagent or reaction of the combination used in the method of the present invention, is a hydrochloride of 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide (EHD) or glutaraldehyde.

In yet another embodiment of the fiber is wound while the continuous drawing. This makes it possible to obtain and store long fibers.

In a second aspect, the present invention relates to a spinning solution for implementing the method of the present invention, comprising, essentially consisting of or consisting of: (i) a polymer which may be introduced into the aqueous solution with the concentration of that component, at least 0.15 mg/ml, (ii) compounds, which increases the longitudinal viscosity of the spinning solution, and (iii) a solvent.

In this context, the specifics�and preferred the polymer would be a polypeptide defined above silk.

In addition, particularly preferred that the concentration of the polymer, for example, the silk polypeptide, would be at least 0.15 mg/ml and not more than 60 mg/ml, more preferably at least 0.15 mg/ml and not more than 50 mg/ml, and most preferably at least 0.15 mg/ml and not more than 20 mg/ml.

Also particularly preferred that the concentration of compound that increases the elongation viscosity of the spinning solution is in the range from 0.1% (wt./about.) up to 5% (wt./vol.), more preferably in the range from 0.5% (wt./about.) up to 4% (wt./vol.), and most preferably in the range from 1% (wt./about.) up to 3% (wt./vol.).

In particular, it is even more preferred that the concentration of the polymer, for example, the silk polypeptide, would be at least 0.15 mg/ml and not more than 60 mg/ml, more preferably at least 0.15 mg/ml and not more than 50 mg/ml, and most preferably at least 0.15 mg/ml and not more than 20 mg/ml, and the concentration of compound that increases the elongation viscosity of the spinning solution is in the range from 0.1% (wt./about.) up to 5% (wt./vol.), more preferably in the range from 0.5% (wt./about.) up to 4% (wt./vol.), and most preferably in the range from 1% (wt./about.) up to 3% (wt./vol.).

In the third aspect, the present invention provides a fiber obtained by the method of the first aspect.

In a fourth aspect the present invention provides products comprising fiber of the second aspect, such as

(i) a thread or

(ii) a woven or nonwoven material material.

In one additional aspect, the present invention provides the use of a fiber or filament comprising one or more cells, for analysis of one or more functions of cells and/or storing the above cells. Preferably, the analysis of cell function is carried out before, during and/or after exposure to one or more cells of the test compound or stimulus, preferably mechanical, thermal and/or electrical stimulus. Fibres comprising cells, could also serve as a frame material for tissue engineering and cultivation of artificial organs.

The present invention improves predmosti polymer solution, making feasible�m getting the entire range of new materials. The present invention is particularly well-suited for inclusion of the living and non-living biological material, since the method can be implemented in appropriate conditions used for temperature, pressure, solvent and chemical reagents.

Because in this way the fibers may be included in a General case, all of the proteins in such fibers may be included in principle, any enzymatic activity. Maybe more important is the fact that fiber can also be embedded cells and so, as has been demonstrated for inclusion in fiber colloidal particles of micron size. Because conditions are favorable for cell viability, are possible applications in bioengineering and growing tissues. Fibres comprising cells, could serve as a frame material for tissue engineering and cultivation of artificial organs. In addition, the encapsulation of living cells makes possible the exposure of these cells to different environmental conditions, e.g. by pulling them through a bath of chemicals. In the presence of such approaches can be made available new tools for cell biology. In this spirit, the invention can be used for consistent and high-performance manipulation with cell�and in a continuous chain. One possibility is to conduct fiber hoods when introducing cells from a spinning solution containing a biologically active compound, and screening of cells as they are released from the solution. Thus, the position on the chain forms a cell index, forming new approaches to high-performance single-celled screening tests. In addition to this, are possible areas of application in the healing of wounds. For example, the fibers comprising cells, secreting factors wound healing, could be incorporated into bandages or xerogels or complement, in particular, in the context of the wet healing of wounds. You can imagine and also options to use when receiving skin grafts, reconstruction of ligaments or surgical mesh. In addition, the fibers obtained in accordance with the invention, can be used in a wide range of other commercial products, for example in the case of rope, nets, apparel textiles, building material, tent fabric, backpacks and more, where desirable characteristics are strength, elasticity and low weight.

The following figures and examples are merely illustrations of the present invention and should in no way be construed as limiting the scope of invention, as specified in the attached FD�mule invention.

Brief description of figures

Figure 1demonstrates the fiber subjected to the extraction of a spinning solution containing 5 mg/ml FITZ-C16and 0.5% (wt./about.) PAA. The needle of colorless glass pull from aliquots of the spinning solution (A)
the result yields a thin fluid elementary fiber (B). (C) Fiber subjected to stretching at a speed equal to at least 10 cm/sec, have a smooth and uniform appearance. (D) Fiber subjected to stretching at a speed lower than the appropriate threshold speed. A drop of liquid still form a coating fluid elementary fiber and stored after deposition of fibers on a clean a glass microscope slide.
Figure 2demonstrates the fiber subjected to the extraction of a spinning solution containing approximately 107/ml polystyrene pellets (diameter 1 μm) dispersed in the solution at 5 mg/ml C16and 0.5% (wt./about.) PAA. The granules are included in fiber and are distributed fairly evenly.
Figure 3demonstrates obtained by the method of atom�about force microscopy image fiber subjected to a drawing process using a spinning solution containing polystyrene granules (diameter 1 μm) dispersed in solution at 5 mg/ml C16and 0.5% (wt./about.) PAA.
Figure 4Pellets covered with fiber material and tightly connected with fiber. Demonstrates Zein fiber subjected to the extraction of a spinning solution containing 300 mg/ml Zein and 0.5% (wt./about.) PAA in 63,75% ethanol. Fiber Zein showed a smooth surface.

Examples

The following examples are intended for illustrative purposes only and in no way limit the invention described above.

Example 1: the Principle of the method hoods

Figure 1A shows an aliquot of the spinning solution consisting of C16as the polymer component, the PAA as a polymer that improves the longitudinal viscosity, and water as a solvent, on a microscope slide in contact with the needle of colorless glass as a tool for drawing. Pulling the needle that is in contact with the spinning solution from the solution yields a thin fluid elementary fiber. This elementary fiber at a sufficiently fast drawing exists for a long enough period of time to ensure evaporated�I water as the solvent and obtain a thin and light fibers (figure 1B). The fibers contain protein, which can be demonstrated by the methods of IR spectroscopy and fluorescence microscopy using the labeled protein.

Example 2: Fiber one protein of spider silk low concentration

100 μl of the spinning solution (10 mg/ml FITZ-C16, and 1.0% (wt./about.) PAA) was placed on a microscope slide. The needle of colorless glass (length 5 cm and a diameter of 1 mm) was injected into contact with the spinning solution, and then took his hand to the glass of the microscope at variable speeds. This method as a result led to the pulling of fibers from a spinning solution, the quality of the fiber used depended on speed. When the pulling speed of 10 cm/sec or more, the fibers have a smooth and uniform appearance (figure 1C). In the case of carrying out the extrusion at speeds that are lower than the threshold, a drop of liquid still form a coating fluid elementary fiber and preserved after deposition of fibers on a clean a glass microscope slide (figure 1D). When the pulling speed of 10 cm/sec or more, was getting good fiber.

Example 3: Fiber, pulling the falling steel pellet

100 μl of the spinning solution (10 mg/ml C16, and 1.0% (wt./about.) PAA) was placed near the edge of a glass slide of a microscope. IU�Doo edge and the spinning solution was placed steel pellet with a diameter of 1 mm, in contact with the spinning solution. While holding the slide of the microscope arm glass slightly tilted, causing the pellets fall off the edge. It is surprising, but the falling pellets were pulling the fiber from the spinning solution is almost the same as the needle is shown in example 1. Way to drop the ball and the receiving fiber can be matched with the fall of the spider-producing fiber, although, obviously, the tank spinning syrup is at different ends of the fiber.

Example 4: Implementation of granules in fiber

100 μl of the spinning solution (10 mg/ml C16, and 1.0% (wt./about.) PAA) was dispersively approximately 107/ml product Dynabeads (granules of polystyrene or PS) with a diameter of 1 μm. The needle of colorless glass (length 5 cm and a diameter of 1 mm) was injected into contact with the spinning solution, and then took his hand to the glass of the microscope at a speed equal to approximately 10 cm/sec. This method as a result led to the extrusion of the spinning solution fibres comprising pellets of PS. The pellets were introduced into the fiber and is distributed fairly evenly (figure 2). Atomic force microscopy demonstrated that the coating of the granules fiber material and their tight coupling with the fiber (figure 3).

Since this experiment can be conducted under conditions suited to living cells by temperature, pressure and Sol�the accelerator, it demonstrates the possibility of including cells used instead of pellets from the SS, which had a diameter similar to the diameter of many cells, such as fibroblasts.

Example 5: Fiber from Zein

Zein is a spare protein from corn and in the quality of the material it was used for decades. It is available with reasonable purity in large quantities at low cost (Tsai 1979). 300 mg/ml Zein in 85% ethanol mixed with 2% (wt./about.) PAA, wherein the final concentration of PAA was 0.5% (wt./vol.). 100 μl of this spinning solution was placed on a microscope slide. The needle of colorless glass (length 5 cm and a diameter of 1 mm) was injected into contact with the spinning solution, and then took his hand to the glass of the microscope at a speed equal to approximately 10 cm/sec. This method as a result led to the extrusion of the spinning solution of Zein fibers (figure 4). Such Zein fibers were insoluble in water and had a smooth surface. They, apparently, showed good mechanical stability, but were rather brittle and unyielding. Fiber Zein could be made more pliable formaldehyde in the bath.

Example 6: the Inclusion of fiber crystallites

In the spinning solution (10 mg/ml C16, and 1.0% (wt./about.) PAA) in suspension in the form of tanked�spirtnogo powder was added dyes (stanovy red (Sigma 20161-8) or Nile red (Fluka 72485)). Both dye was introduced into the fibers. Both of the dye are hydrophobic and firmly stick to hydrophobic proteins in spider silk.

Example 7: the Inclusion in fiber enzymes

In the fiber (10 mg/ml C16, and 1.0% (wt./about.) PAA) include fluorescent proteins such as green fluorescent protein (GFP). After enabling saw a bright fluorescence. It still shows the sincerity of stacking protein (GFP) in the fibers and therefore the protein itself.

In the fiber (10 mg/ml C16, and 1.0% (wt./about.) PAA) include β-galactosidase. As a result of enzymatic hydrolysis hydrolysis of o-nitrophenyl-β-D-galactopyranoside (ONPG) to form a yellow-nitroanaline dye. Set the concentration of o-NITROPHENOL to quantify the activity of β-galactosidase in the fiber. The inclusion of enzymes can be used for any applications that require enzymes that are large enough to trap in the fiber while the possibility of diffused matter inside and out.

1. Method of spinning fibers from a spinning solution comprising the stage of:
(a) obtain a spinning solution containing (i) a polymer that can be injected in an aqueous solution with a concentration of the constituent of at least 0.15 mg/ml, (ii) polyacrylamide (PAA), and (iii) a solvent; and
(b) drawing the fiber from a spinning solution or combination of extrusion and drawing fibers from a spinning solution, in the resulting fiber.

2. A method according to claim 1, wherein the polymer is a polypeptide, preferably, the silk polypeptide comprising at least two identical repetitive element, bovine serum albumin (BSA), Zein or casein.

3. A method according to claim 2, where the silk polypeptide comprises at least two identical repetitive element, each of which includes at least one consensus sequence selected from the group consisting of:
(i) GPGXX (SEQ ID NO:3), where X represents any amino acid, preferably in each case independently selected from A, S, G, Y, P, N and Q;
(ii) GGX, where X represents any amino acid, preferably in each case independently selected from Y, P, R, S, A, T, N and Q; and
(iii) Axwhere x is an integer in the range from 5 to 10.

4. A method according to claim 3, wherein the repeating unit is independently selected from module A (SEQ ID NO: 20), module C (SEQ ID NO: 21), Q (SEQ ID NO: 22), module (SEQ ID NO: 23), module sp (SEQ ID NO: 24), module S (SEQ ID NO: 25), module R (SEQ ID NO: 26), module X (SEQ ID NO: 27) or module Y (SEQ ID NO: 28) or their variants.

5. A method according to claim 2, where the silk polypeptide further comprises at least one non-repetitive (NR) link.

6. A method according to claim 5, where the link NR represents NR3 (SEQ ID NO: 41) or a variant thereof, or NR4 (SEQ ID NO: 42) or a variant thereof.

7. A method according to claim 1, wherein the concentration�imera is in the range from 0.15 mg/ml to 350 mg/ml, preferably in the range from 0.5 mg/ml to 50 mg/ml, and more preferably in the range from 1 mg/ml to 20 mg/ml.

8. A method according to claim 1, wherein the polyacrylamide (PAA) covalently linked to the polymer.

9. A method according to claim 1, wherein the concentration of polyacrylamide (PAA) is in the range from 0.1% (wt./about.) up to 5% (wt./vol.).

10. A method according to claim 1, wherein the solvent is selected from the group consisting of a polar solvent, preferably water, aqueous buffer or alcohol; preferably isopropanol, hexafluoroisopropanol, glycerol, ethanol (EtOH), propanol, butanol, octanol, non-polar solvent, preferably hexane, dodecane, oils, acetone or other organic solvents, preferably ethyl acetate; and mixtures thereof.

11. A method according to claim 1, wherein the fiber hood initiate the introduction of interfacial surface air/liquid from the solution in contact with the tool for extraction and removal tool for drawing air from the interfacial surface.

12. A method according to claim 1, wherein the extraction is carried out at speeds of at least 0.1 cm/sec, preferably 10 cm/sec, and more preferably 10 m/sec.

13. A method according to claim 1, wherein the spinning solution further comprises a compound that increases the Newtonian viscosity, preferably monosaccharides, polysaccharides or polyols.

14. A method according to claim 1, wherein the spinning solution additional�Uo contains dispersed therein particulate material.

15. A method according to claim 14, where the particulate material is selected from the group consisting of cells, granules, metals that conduct electricity, crystallites, complexes of protein/protein and enzymes or growth factors.

16. A method according to claim 14, where the dispersed material in the spinning solution is present in amounts in the range from 0.01% (wt./about.) up to 10% (wt./vol.), preferably from 0.5% (wt./about.) up to 1% (wt./vol.).

17. A method according to claim 1, wherein the method after step (b) includes a step (C) curing the fiber in a curing solution or staple fiber.

18. Spinning solution for implementing the method according to claims.1-17 containing (i) a polymer that can be injected in an aqueous solution with a concentration of the constituent of at least 0.15 mg/ml, (ii) polyacrylamide (PAA), and (iii) a solvent.

19. The fiber obtained by the method according to claims.1-17.

20. The yarn comprising the fiber according to claim 19.

21. Woven or non-woven fabric comprising the fiber according to claim 19.

22. The use of a fiber according to claim 19 or filament according to claim 20 comprising one or more cells, to save the above cells, where the cells included in them.

23. The use according to claim 22, where the one or more cells is used (i) in screening cells to identify one or more cell functions;
(ii) as a frame material for tissue engineering and cultivation of artificial organs and/or (iii) when healed�attachment wounds.

24. The use according to claim 23, where the analysis of cell function is carried out before, during and/or after exposure to one or more cells of the test compound or stimulus, preferably mechanical, thermal and/or electrical stimulus.



 

Same patents:

FIELD: textiles, paper.

SUBSTANCE: fire resistant yarn comprises the fibre based on polyarylate and the fibre on acrylic base, comprising antimony compound, also contains from 1 to 30 wt % fibre based on polyarylate relating to the total weight of the fire resistant yarn. The proposed fire resistant fabric comprises a fibre based on polyarylate and the fibre on acrylic base, comprising antimony compound, also contains from 1 to 30 wt % fibre based on polyarylate relating to the total weight of the fire resistant fabric. The proposed clothing and the fire resistant workwear comprises the fire resistant fabric.

EFFECT: low cost of fire resistant yarn, fire resistant fabric, and fire resistant workwear, excellent aesthetic characteristics and fire-resistant properties.

19 cl

FIELD: textiles, paper.

SUBSTANCE: invention provides a fishing line comprising a composite thread consisting of a core part comprising a short fiber and a shell part comprising a filament yarn made of synthetic fibers, and the core part and the shell part are joined due to indumentum of short fibers, formed between the long fibers or braided with them, and the specific mass of the thread can be adjusted in the range of 1.0 or more, and a method of manufacturing the fishing line.

EFFECT: tight structure, separation or delamination of the core part and the shell part is not allowed, ease of use and excellent durability, weather resistance and water resistance.

23 cl

FIELD: textiles, paper.

SUBSTANCE: bicomponent fibers contain aliphatic polyester or a mixture of aliphatic polyesters, which form the first component, and polyolefin or a mixture of polyolefins, which form the second component. Polyolefin contains auxiliary material improving its biodegradation. Textile sheets include these bicomponent fibers and are comparable by mechanical properties to textile sheets based on polyolefin, while they are decomposed more efficiently under the action of microorganisms than the textile sheets based on polyolefin.

EFFECT: enhanced biodegradability, to textile sheets such as nonwoven materials comprising these fibers, which can be used in personal care products.

16 cl, 3 tbl, 2 ex

FIELD: textile, paper.

SUBSTANCE: yarn for woven and jersey articles is characterized by the following composition of components, wt %: - heat resistant polyamide imide or polymethaaramide fibre 45-55; - heat resistant polyparaaramide fibre 2-4; - antistatic fibre 1-2; - fire resistant viscose fibre - balance. Polyamide imide fibre is represented by Kermel fibre, polymethaaramide fibre - by Nomex, Conex or Newstar, polyparaaramide fibre - by Kevlar or Tvaron, antistatic fibre - by Bekinox, fire resistant viscose fibre - by Lenzing or Avylon.

EFFECT: invention makes it possible to reduce heat shrinkage and specific surface electric resistance of yarn, to increase its oxygen index, and to expand its functional capabilities.

1 tbl, 5 cl

FIELD: textile industry.

SUBSTANCE: yarn from collagen fibre of animal skin contains 1÷100% of collagen fibre by weight, which is made of loosened collagen fibre produced by release of fibre in at least one type of finished skin or hides of at least one type of animals, and 0÷99% of textile fibre by weight. Textile fibre and collagen fibre are twisted together. Collagen fibre is produced from at least one type of animals, including cattle, sheep, horses, dogs, pigs, deer, rabbits, crocodiles and snakes. Textile fibre represents at least one type of natural or synthetic fibres, including cotton, hemp, wool, silk, terylene, acryl fibre, nylon, polyamide and viscose staple. Method for manufacturing of yarn from collagen fibre of animal skin includes selection of tanned leather materials, release of fibres, sorting, mixing, combing, drawing and twisting. Loosener is used to release fibre, and box-like separator with air flow is used for fibre sorting. In version of method realisation the following operations are carried out - selected of non-tanned leather materials, liming, washing with water, de-ashing, tanning and softening, dehydration, release of fibres, sorting, mixing, combing, drawing and twisting. Acid protease is used for de-ashing, and pH value of de-ashing solution is controlled within the limits from 3 to 6. Box-like separator with air flow is used for sorting of fibre. In other version of method realisation raw materials are selected from materials of tanned leather and at least one of synthetic textile fibres or natural textile fibres, release of collagen fibres for production of loosened collagen fibres with single thread, sorting of loosened collagen fibres, mixing of collagen fibres and textile fibres with further combing of mixed fibres for production of continuous fibre, drawing of fibre for improved homogeneity of fibres and twisting of fibres with production of yarn. Box-like separator with air flow is used for sorting of fibre.

EFFECT: produced yarn has high tensile strength, wear resistance, softness, moisture- and oil-absorption and fire-resistance, which makes it possible to use it in weaving, knitting and plaiting, it is possible to produce high-quality cloth from yarn for four seasons with high graph and high strength, which considerably widens sphere of animal skin application and improves extent of its usage.

7 cl, 1 dwg

FIELD: textiles, paper.

SUBSTANCE: group of inventions relates to manufacturing of the combined polyester thread. Polyester combined filament thread consists of self-extensible polyester complex thread A and heat-shrinkable polyester complex thread B. Polyester complex thread contains a medullary part and an assemblage of costal parts running in the radial direction from the medullary part along the longitudinal direction of the medullary part, and simultaneously meets the below-mentioned conditions (a)-(c): (a) 1/20≤SB/SA≤1/3; (b)0.6≤LB/DA≤3.0; (c) WB //DA≤1/4; whereSA - cross-sectional area of the medullary part,DA - diameter of the medullary part when its cross-section is circle, and diameter of a circumscribed circle when it is not circle, and SB,LB and WB are the area of cross-section, maximum length and maximum width of costal parts, respectively.

EFFECT: production of clothing possessing high elasticity, excellent softness, and dry-by-touch properties.

6 cl, 2 dwg

FIELD: textile industry.

SUBSTANCE: method comprises moulding fluff-feather thread from raw material by means of withdrawing the raw material, combing the raw material to form fluff-feather fibers, twisting the fibers into thread, winding the thread, and heat treatment of the wound thread.

EFFECT: improved method.

15 cl, 1 dwg

FIELD: process or apparatus for producing yarns or threads.

SUBSTANCE: fireproof yarn comprises fireproof polyether fiber or the mixture of, in mass %, 30-100 of the fireproof polyether fiber with 0-70 of the other fireproof fibers. The linear density of the yarn is 18.5-50 tex. The linear density of the fire-proof fibers is 0.13-0.15 tex or 0.2-0.3 tex.

EFFECT: improved refractoriness.

1 tbl

FIELD: filament fibrous material in the form of reinforced shoe, knitting and embroidery threads used in sewing industry, shoe production and other branches of industry.

SUBSTANCE: filament fibrous material contains 25-39.6 wt% of cotton and siblon, 24.45-75 wt% of polyester filament, 0.3-0.5 wt% of soaking agent and 0.05-0.1 wt% of aromatizer. According to one of versions, material contains 35-55 wt% of cotton, 20-30 wt% of siblon, 24.3-44.2 wt% of viscose high-module filament, 0.2-0.3 wt% of soaking agent and 0.45-0.5 wt% of aromatizer.

EFFECT: reduced breakage of filaments in the process of sewing and winding owing to reduced fluffiness and decreased friction, and provision for imparting aromatic properties to material.

3 cl, 1 dwg, 2 tbl

FIELD: textile yarn for manufacture of various comfortable fire-resistant articles.

SUBSTANCE: textile yarn contains twisted thermally oxidized polyacrylonitrile filaments or twisted thermally oxidized polyacrylonitrile filaments mixed with other filaments. Thermally oxidized polyacrylonitrile filaments have linear density of 0.11-0.5 tex, length of 40-90 mm, twist rate of 3-7 twists per 1 cm of length, and density of 1.37-1.43 g/cm3, and are mixed with animal or plant fibers, or with fire-resistant viscose, aramide, paraaramide, polyoxodiazole filaments, or mixture thereof. Share of twisted thermally oxidized polyacrylonitrile filaments in mixtures constitutes at least 25% by weight of yarn. Yarn may additionally comprise core of paraaramide or polyoxodiazole continuous thread.

EFFECT: improved operating characteristics, increased resistance to open fire, moisture and intermingling of filaments, reduced production cost and provision for manufacture of highly comfortable articles from yarn of such structure.

3 cl, 2 tbl

FIELD: medicine.

SUBSTANCE: recombinant method is used to produce a spidroin protein of a principal ampullary gland which consists of 150-420 amino acid residues and is described by formula REP-CT where REP is a protein fragment consisting of 80-300 amino acid residues, selected from L(AG)nL, L(AG)nAL, L(GA)nL or L(GA)nGL where n is an integer from 4 to 8. Each individual segment A consists of 8-18 amino acid residues, where 0 to 3 amino acid residues are not Ala, while the rest are Ala. Each individual segment G consists of 12-30 amino acid residues, where at least 40% of amino acid residues are Gly. Each individual segment L is a linker amino acid sequence of 0-20 amino acid residues. CN is a fragment consisting of 70 to 120 amino acid residues of a C-terminal spidroin protein fragment of the principal ampullary gland.

EFFECT: invention presents the polymerisable spidroin protein of the principal ampullary gland which is used as a basis to produce the controlled polymerisable fused protein.

15 cl, 7 dwg, 13 ex

FIELD: chemistry.

SUBSTANCE: method involves preparation of silk fibroin, including grinding, dissolution in lithium bromide while heating, dialysis with removal of lithium bromide from the dissolved silk fibroin through a semipermeable membrane, drying to form a film, followed by dissolution thereof in 1,1,1,3,3,3-hexafluoro-2-propanol, and then mixing with dissolved polymethylmethacrylate in 1,1,1,3,3,3-hexafluoro-2-propanol. The film is then cast on a fluoroplastic substrate with removal of solvent, thereby forming a 60-70 mcm thick film, followed by drying at temperature 30-35°C for 5-6 hours with forced ventilation, with subsequent treatment in ethanol while vertically immersing the film into a bath at a frequency of 15-20 immersions per hour, for 15-20 minutes.

EFFECT: high strength, optical transmission coefficient, oxygen permeability, while retaining moisture content, limiting wetting angle in film materials for making soft contact lenses.

5 cl, 4 tbl

FIELD: cellulose derivatives.

SUBSTANCE: invention relates to technology of manufacturing fibers and films from mixtures of natural polymers: cellulose and fibroin, which can be used, for instance, in fabrication of linen assortment articles. Process comprises preparing separately cellulose and fibroin solutions in organic solvent followed by regeneration and drying. Wood cellulose having degree of polymerization 200-400 is used. Both polymers are dissolved to concentration 5-15 wt % in ionic solvent, which is composed of following cation: , wherein R1 is ethyl or butyl, and chloride or acetate anion. Dissolution is accompanied by turbulent stirring at 60-90°C until dissolution is completed. Details: cellulose/fibroin ratio in their mixture is between 95:5 and 60:40; rotation speed of stirrer is 600 to 1200 rpm; stirrer blades reciprocate in vertical direction at amplitude 200 to 2000 mm and frequency 0.125 s-1; and regeneration of polymer is effected via precipitation into water or water-organic bath.

EFFECT: enhanced bacteriostatic properties of material and increased its strength in wet state when operated.

2 cl, 1 dwg, 3 tbl, 18 ex

The invention relates to a process for the production of fibers and films, in particular to a method of dissolving silk with obtaining solutions which are suitable for processing in the molding product

FIELD: chemistry.

SUBSTANCE: claimed are filaments, containing filament-forming material and an additive, non-woven cloths and methods of obtaining such filaments. Filament and/or fibre contain filament-forming material and an additive, such as active agent, which produces desired effect in medium, outside filament and/or non-woven cloth, containing said filament, when filament is subjected to impact of conditions of target application of filament and/orfilament-containing non-woven cloth.

EFFECT: obtaining filaments, containing filament-forming material and an additive.

39 cl, 6 dwg

FIELD: chemistry.

SUBSTANCE: claimed are filaments, containing filament-forming material and additive, non-woven cloths and method of obtaining such filaments. Filament and/or fibre contain filament-forming material and additive, such as active agent, which produces desirable effect in medium, outside filament and/or non-woven cloth, containing said filament, when filament is subjected to impact of conditions of target application of filament and/or filament-containing non-woven cloth.

EFFECT: obtaining filaments.

44 cl, 6 dwg, 20 tbl

FIELD: chemistry.

SUBSTANCE: claimed are filaments, containing filament-forming material and an additive, non-woven cloths and methods of obtaining said filaments. Filament and/or fibre contain filament-forming material and an additive such as active agent, which produces desired effect in medium, outside filament and/or non-woven cloth, containing said filament, when filament is subjected to impact of conditions of target application of filament and/or non-woven filament-containing cloth.

EFFECT: obtaining filaments, containing filament-forming material and an additive.

40 cl, 6 dwg

FIELD: chemistry.

SUBSTANCE: formed fibres are subjected to thermal processing in an air medium with heating. The fibres with introduced carbon nanoparticles, which are represented by technical carbon in an amount of 0.2-10%, with the surface, containing oxygen in an amount not less than 4.8 atomic %, are subjected to oxidative stabilisation with an increase of temperature from 180 to 230°C at a rate of 0.5°C per minute for 90-110 minutes.

EFFECT: complete performance of the process of oxidative stabilisation of PAN fibres, filled with technical carbon, simplification of the technology due to reduction of the time of the process performance, with the simultaneous reduction of heat conductivity by the fibres, achieved due to the introduction of technical carbon into the fibres, which is necessary for further obtaining of a carbon material, used as a heat insulator for furnaces of an inert medium.

1 tbl, 5 ex

FIELD: chemistry.

SUBSTANCE: moulded fibres are subjected to heat treatment in an air medium while heating and maintaining a constant length. Content of carbon nanotubes in the fibres is 0.3-0.5%. The surface of the nanotubes contains oxygen in amount of not less than 3.5 at %. Oxidative stabilisation is carried out by raising temperature from 180°C to 230°C at a rate of 0.5°C per minute for 110-130 minutes.

EFFECT: simple technique owing to shorter process duration and improved strength properties of polyacrylonitrile fibres owing to low content of carbon nanotubes.

1 tbl, 7 ex

FIELD: chemistry.

SUBSTANCE: method of obtaining a thermally stable nanocomposite polyethyleneterephthalate fibre due to the modification of an initial polymer with carbon nanotubes, including heating in a thermostatted mixer until melt is obtained, with constant mixing, and the supply of nanotubes to the melt, the polymer hardening, applying it to obtain, in particular, by crushing, granules, placing them into an extruder and formation of fibre, is characterised by the fact, that to melting subjected is a tenth part of the polymer, separated from the total volume, with the supply into it of a water solution of the carbon nanotubes, processed with ultrasound, with further mixing of the obtained hardened polymer granules with the remaining part of the initial polymer.

EFFECT: obtaining the nanocomposite polyethylenetereohthalate fibre with higher indices of thermal stability with minimal expenditures for its production.

1 tbl

FIELD: chemistry.

SUBSTANCE: invention relates to technology of obtaining ultrathin polymer fibres by method of electrospinning and can be used for spinning non-woven porous fibrous materials, applied as separating partitions, for instance, for filtration of gases and liquids, for manufacturing diffusion partitions, separators of chemical sources of current, etc. Solution for spinning contains 2.5-4 wt.p. of phenolformaldehyde resin, 2.5-4 wt.p. of polyvinyl butyral, 92-95 wt.p. of ethyl alcohol and as modifying additives 0.02-0.2 wt.p. of tetrabutylammonium iodide or 0.01-0.1 wt.p. of lithium chloride.

EFFECT: invention provides increase of solution electroconductivity, increased output of ultrathin fibres with diameter less than 0,1 mcm.

1 tbl, 7 ex

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