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WO2010072665A1 - Modification de nanofibres ou de mésofibres ou de produits textiles plats produits par électrofilage à l'aide de protéines amphiphiles - Google Patents

Modification de nanofibres ou de mésofibres ou de produits textiles plats produits par électrofilage à l'aide de protéines amphiphiles Download PDF

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Publication number
WO2010072665A1
WO2010072665A1 PCT/EP2009/067492 EP2009067492W WO2010072665A1 WO 2010072665 A1 WO2010072665 A1 WO 2010072665A1 EP 2009067492 W EP2009067492 W EP 2009067492W WO 2010072665 A1 WO2010072665 A1 WO 2010072665A1
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WO
WIPO (PCT)
Prior art keywords
copolymers
polymer
nano
proteins
amphiphilic
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Application number
PCT/EP2009/067492
Other languages
German (de)
English (en)
Inventor
Burghard Liebmann
Evgueni Klimov
Gero Nordmann
Original Assignee
Basf Se
Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.)
Filing date
Publication date
Application filed by Basf Se filed Critical Basf Se
Publication of WO2010072665A1 publication Critical patent/WO2010072665A1/fr

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Classifications

    • D—TEXTILES; PAPER
    • D01—NATURAL OR MAN-MADE THREADS OR FIBRES; SPINNING
    • D01D—MECHANICAL METHODS OR APPARATUS IN THE MANUFACTURE OF ARTIFICIAL FILAMENTS, THREADS, FIBRES, BRISTLES OR RIBBONS
    • D01D5/00—Formation of filaments, threads, or the like
    • D01D5/0007—Electro-spinning
    • D01D5/0015—Electro-spinning characterised by the initial state of the material
    • D—TEXTILES; PAPER
    • D01—NATURAL OR MAN-MADE THREADS OR FIBRES; SPINNING
    • D01F—CHEMICAL FEATURES IN THE MANUFACTURE OF ARTIFICIAL FILAMENTS, THREADS, FIBRES, BRISTLES OR RIBBONS; APPARATUS SPECIALLY ADAPTED FOR THE MANUFACTURE OF CARBON FILAMENTS
    • D01F1/00—General methods for the manufacture of artificial filaments or the like
    • D01F1/02—Addition of substances to the spinning solution or to the melt
    • D01F1/10—Other agents for modifying properties
    • D—TEXTILES; PAPER
    • D01—NATURAL OR MAN-MADE THREADS OR FIBRES; SPINNING
    • D01F—CHEMICAL FEATURES IN THE MANUFACTURE OF ARTIFICIAL FILAMENTS, THREADS, FIBRES, BRISTLES OR RIBBONS; APPARATUS SPECIALLY ADAPTED FOR THE MANUFACTURE OF CARBON FILAMENTS
    • D01F6/00—Monocomponent artificial filaments or the like of synthetic polymers; Manufacture thereof
    • D01F6/02—Monocomponent artificial filaments or the like of synthetic polymers; Manufacture thereof from homopolymers obtained by reactions only involving carbon-to-carbon unsaturated bonds
    • D—TEXTILES; PAPER
    • D01—NATURAL OR MAN-MADE THREADS OR FIBRES; SPINNING
    • D01F—CHEMICAL FEATURES IN THE MANUFACTURE OF ARTIFICIAL FILAMENTS, THREADS, FIBRES, BRISTLES OR RIBBONS; APPARATUS SPECIALLY ADAPTED FOR THE MANUFACTURE OF CARBON FILAMENTS
    • D01F6/00—Monocomponent artificial filaments or the like of synthetic polymers; Manufacture thereof
    • D01F6/28—Monocomponent artificial filaments or the like of synthetic polymers; Manufacture thereof from copolymers obtained by reactions only involving carbon-to-carbon unsaturated bonds
    • D—TEXTILES; PAPER
    • D01—NATURAL OR MAN-MADE THREADS OR FIBRES; SPINNING
    • D01F—CHEMICAL FEATURES IN THE MANUFACTURE OF ARTIFICIAL FILAMENTS, THREADS, FIBRES, BRISTLES OR RIBBONS; APPARATUS SPECIALLY ADAPTED FOR THE MANUFACTURE OF CARBON FILAMENTS
    • D01F6/00—Monocomponent artificial filaments or the like of synthetic polymers; Manufacture thereof
    • D01F6/28—Monocomponent artificial filaments or the like of synthetic polymers; Manufacture thereof from copolymers obtained by reactions only involving carbon-to-carbon unsaturated bonds
    • D01F6/36—Monocomponent artificial filaments or the like of synthetic polymers; Manufacture thereof from copolymers obtained by reactions only involving carbon-to-carbon unsaturated bonds comprising unsaturated carboxylic acids or unsaturated organic esters as the major constituent
    • D—TEXTILES; PAPER
    • D01—NATURAL OR MAN-MADE THREADS OR FIBRES; SPINNING
    • D01F—CHEMICAL FEATURES IN THE MANUFACTURE OF ARTIFICIAL FILAMENTS, THREADS, FIBRES, BRISTLES OR RIBBONS; APPARATUS SPECIALLY ADAPTED FOR THE MANUFACTURE OF CARBON FILAMENTS
    • D01F6/00—Monocomponent artificial filaments or the like of synthetic polymers; Manufacture thereof
    • D01F6/28—Monocomponent artificial filaments or the like of synthetic polymers; Manufacture thereof from copolymers obtained by reactions only involving carbon-to-carbon unsaturated bonds
    • D01F6/42—Monocomponent artificial filaments or the like of synthetic polymers; Manufacture thereof from copolymers obtained by reactions only involving carbon-to-carbon unsaturated bonds comprising cyclic compounds containing one carbon-to-carbon double bond in the side chain as major constituent
    • D—TEXTILES; PAPER
    • D01—NATURAL OR MAN-MADE THREADS OR FIBRES; SPINNING
    • D01F—CHEMICAL FEATURES IN THE MANUFACTURE OF ARTIFICIAL FILAMENTS, THREADS, FIBRES, BRISTLES OR RIBBONS; APPARATUS SPECIALLY ADAPTED FOR THE MANUFACTURE OF CARBON FILAMENTS
    • D01F6/00—Monocomponent artificial filaments or the like of synthetic polymers; Manufacture thereof
    • D01F6/44—Monocomponent artificial filaments or the like of synthetic polymers; Manufacture thereof from mixtures of polymers obtained by reactions only involving carbon-to-carbon unsaturated bonds as major constituent with other polymers or low-molecular-weight compounds
    • D—TEXTILES; PAPER
    • D01—NATURAL OR MAN-MADE THREADS OR FIBRES; SPINNING
    • D01F—CHEMICAL FEATURES IN THE MANUFACTURE OF ARTIFICIAL FILAMENTS, THREADS, FIBRES, BRISTLES OR RIBBONS; APPARATUS SPECIALLY ADAPTED FOR THE MANUFACTURE OF CARBON FILAMENTS
    • D01F6/00—Monocomponent artificial filaments or the like of synthetic polymers; Manufacture thereof
    • D01F6/58—Monocomponent artificial filaments or the like of synthetic polymers; Manufacture thereof from homopolycondensation products
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61L—METHODS OR APPARATUS FOR STERILISING MATERIALS OR OBJECTS IN GENERAL; DISINFECTION, STERILISATION OR DEODORISATION OF AIR; CHEMICAL ASPECTS OF BANDAGES, DRESSINGS, ABSORBENT PADS OR SURGICAL ARTICLES; MATERIALS FOR BANDAGES, DRESSINGS, ABSORBENT PADS OR SURGICAL ARTICLES
    • A61L2400/00—Materials characterised by their function or physical properties
    • A61L2400/12—Nanosized materials, e.g. nanofibres, nanoparticles, nanowires, nanotubes; Nanostructured surfaces

Definitions

  • the present invention relates to a process for producing nano- or mesofibres and / or textile fabrics comprising nano- or mesofibres comprising the step: i) electrostatic spinning of at least one polymer A, wherein the polymer A is spun in the presence of at least one amphiphilic protein and or the nano- or mesofibers and / or the textile fabric are treated with at least one amphiphilic protein, nano- or mesofibres obtainable by the process according to the invention, textile fabrics obtainable by the process according to the invention and the use of the nano- or mesofibres or the textile sheet.
  • the polymers to be spun first have to be dissolved.
  • non-aqueous solvents For water-insoluble polymers such as polyamides, polyolefins, polyesters or polyurethanes, therefore, non-aqueous solvents must be used.
  • water-soluble polymers such as polyvinyl alcohol, polyethylene oxide, polyvinylpyrrolidone or hydroxypropylcellulose, it is possible to dispense with the use of nonaqueous solvents.
  • the fibers obtained in this way are naturally soluble in water, which is why their technical application is severely limited.
  • WO 2006/089522 A1 relates to a process for the production of polymer fibers, wherein a colloidal dispersion of at least one substantially water-insoluble polymer is electrospun in an aqueous medium.
  • aqueous polymer dispersions it has been possible for the first time to spin aqueous polymer dispersions by means of an electrospinning process, polymer fibers, in particular nano- or mesofibres, being obtained.
  • WO 2008/022993 also relates to a process for producing polymer fibers, wherein colloidal dispersions of at least one essentially water-insoluble polymer are electrospun in an aqueous medium.
  • the colloidal dispersions contain at least one nonionic surfactant.
  • WO 2006/13148 discloses the coating of fibrous substrates selected from textile substrates and leather with hydrophobins.
  • An essential area of application of the nano- or mesofibers produced by electrospinning is the production of textile fabrics containing these nano- or mesofibers. These fabrics can be used in many different applications, for example for the production of filters, non-wovens, nonwovens, technical or household textiles, cleaning products, medical textiles, hygiene products or coatings and / or components of the above-mentioned articles, cell culture carriers Depending on the field of application of the nano- or mesofibers, it is desirable to optimally adjust the hydrophilicity or hydrophobicity of the nano- or mesofibres or of the textile fabrics obtained therefrom. Depending on which electrospinning process is used to produce the nano- or mesofibres, however, it is not possible to adjust the hydrophilicity or hydrophobicity by any selection of the polymers used.
  • the object of the present application is therefore to provide a method for the production of nano- or mesofibres or textile fabrics, wherein the hydrophilicity or hydrophobicity of the nano- or mesofibres or the textile fabrics can be adjusted in a targeted manner, and the provision of the corresponding nano- or mesofibers. or mesofibres or textile fabrics with specifically adjusted hydrophobicity or hydrophilicity.
  • amphiphilic proteins are to be understood as meaning those proteins which have both hydrophilic and hydrophobic regions. Depending on the hydrophilicity or hydrophobicity of the polymer A used, the amphiphilic proteins can thus interact with the hydrophilic region or their hydrophobic region with the polymer A and thus either hydrophilize or hydrophobicize the polymer.
  • the electrostatic spinning of at least one polymer A can be carried out in any manner known to those skilled in the art. That is, the electrostatic spinning comprises electrostatically spinning a polymer melt, a polymer solution, and an aqueous dispersion of a substantially water-insoluble polymer. In the process according to the invention, preference is given to electrostatic spinning of an aqueous dispersion of a substantially water-insoluble polymer.
  • DE-A 196 00 162 and DE-A 10 2004 009 887 and DE-A 10 2006 014 236 disclose processes for the electrospinning of polymer melts.
  • DE-A 101 33 393 and WO 01/09414 and DE-A 103 55 665 relate to processes for the electrospinning of a water-insoluble polymer from a solution. Also in US 6,641,773 B2 an electrospinning process is disclosed in which the polymer is spun from a solution. Alternatively, according to US Pat. No. 6,641,773 B2, electrospinning of the polymer from a polymer melt is possible.
  • WO 2006/089522 and WO 2008/022993 each relate to a process for producing polymer fibers, wherein a colloidal dispersion of at least one essentially water-insoluble polymer is electrospun in an aqueous medium.
  • electrospinning processes from the melt, from solution or from aqueous dispersion, it is possible to produce nanofibres or mesofibres, which are generally obtained directly in the form of textile fabrics.
  • the fabrics are obtained directly during the electrospinning process.
  • the polymer threads formed during the electrospinning process z.
  • a support e.g. a glass carrier or a polymer film or are deposited on a treadmill, for example on a polypropylene substrate, wherein a textile fabric is formed by mixing and interlacing the polymer threads.
  • nano- or mesofibers can be produced or textile fabrics can be obtained directly by the process according to the invention.
  • Any polymers can be used as polymers A, as long as they can be electrostatically spun, either from the melt, from solution or from an aqueous dispersion.
  • Suitable polymers A are, for example, selected from the group consisting of polymers prepared by free-radical polymerization, for example selected from the group consisting of homo- and copolymers of aromatic vinyl compounds such as styrene-homo- or styrene copolymers, homo- and copolymers of alkyl acrylates, Homopolymers and copolymers of alkyl methacrylates, homo- and copolymers of ⁇ -olefins such as polyethylene or polypropylene, homopolymers and copolymers of aliphatic dienes, homo- and copolymers of vinyl halides, homo- and copolymers of vinyl acetates, wherein the homo- and copolymers partially or can be completely hydrolyzed to vinyl alcohols, homo- and copolymers of acrylonitriles, homopolymers and copolymers of vinylamides, polyacetals and copolymers composed of two or more of the above-mentioned poly
  • polyalkylene glycols, polyether polyols or polyalkylene oxides polymers prepared by polyaddition selected from homopolymers and copolymers of urethane biopolymers such as polysaccharides, polylactides, polyglycosides, modified and unmodified celluloses, viscose, chitosan and mixtures of the abovementioned homo- and copolymers.
  • polymers A may be homopolymers or copolymers. These may be unbranched or branched, wherein the branched polymers may be present as star polymers, highly branched polymers or dendrimers.
  • the copolymers may be in the form of random copolymers, block copolymers or graft copolymers. Furthermore, they may be mixtures of two or more of the above polymer types.
  • polymers A can be used in uncrosslinked or in crosslinked form.
  • the polymers may be intermolecularly or intramolecularly crosslinked.
  • Preferably used polymers A are fundamentally dependent on the selected electrospinning process.
  • the polymer A is preferably selected from the group consisting of homopolyamides, copolyamides, homopolyesters, copolyesters, aromatic vinyl compounds, vinyl alcohols, homo- and copolymers of acrylonitriles, polyethers, polycarbonates, homopolymers and Copolymers of urethanes, polylactides and polyglycosides.
  • Suitable solvents for the electrostatic spinning of a polymer solution are all solvents which are capable of dissolving the polymers to be spun under the process conditions of electrospinning. It is further preferred that the solvent can be rapidly removed from the surface of the polymer during spinning to the nano or mesofibers.
  • Suitable solvents are, for example, acetone, alcohols such as methanol, ethanol, propanol, ethers such as ethyl ether and tetrahydrofuran, halogenated solvents such as methylene chloride or chloroform, dimethylformamide, dimethylacetamide, aromatic solvents such as toluene, pyridine, water, ionic liquids or mixtures of the abovementioned Solvent, wherein the solvent used depends on whether the polymer A is soluble in the solvent.
  • the polymer solutions used may, in addition to the polymer A, the solvent and optionally the at least one amphiphilic protein further additives and additives, for example, plasticizers, dyes, pigments, lubricants, antioxidants, stabilizers for UV light, antistatic agents, flame retardants, antimicrobial reagents, Preservatives, surfactants, nucleating agents and other additives known in the art.
  • additives and additives for example, plasticizers, dyes, pigments, lubricants, antioxidants, stabilizers for UV light, antistatic agents, flame retardants, antimicrobial reagents, Preservatives, surfactants, nucleating agents and other additives known in the art.
  • the viscosity of the polymer solution used for electrospinning is generally 0.05 to 20 Pas, preferably 0.1 to 10 Pas. Usually 1 to 40 wt .-%, preferably 2 to 30 wt .-% of the polymer A is dissolved in the solvent or solvent mixture.
  • the temperature of the electrospinning process when using a solution of the polymer A is basically dependent on the solvent used. The process is usually carried out using a polymer solution at temperatures of 5 to 90 ° C., preferably 10 to 60 ° C., very particularly preferably at room temperature.
  • Suitable polymers A which can be electrostatically spun in the melt are known to the person skilled in the art.
  • suitable polymers are homopolyamides, copolyamides, homopolyesters, copolyesters, polyaryl sulfides, polyacetals and homopolymers and copolymers of ⁇ -olefins, for example cycloolefin polymers and mixtures thereof.
  • the polymer melt may contain, in addition to the polymer A and optionally the at least one amphiphilic protein further additives and / or additives.
  • Suitable additives and / or additives are known to the person skilled in the art and correspond to the additives and additives mentioned with regard to the abovementioned polymer solutions.
  • the temperature when carrying out the electrostatic spinning of a polymer melt is dependent on the melting point of the polymer used or of the polymer mixture used.
  • the electrospinning is carried out from the melt at temperatures of generally 90 to 300 0 C, preferably 120 to 250 0 C.
  • Suitable devices for spinning out of the melt are mentioned, for example, in DE-A 196 00 162 and DE-A 10 2004 009 887.
  • Suitable, substantially water-insoluble polymers A which are used in the electrostatic spinning of a colloidal dispersion are known to the person skilled in the art. Suitable polymers are disclosed in WO 2006/089522 and WO 2008/022993.
  • polymers which are substantially water-insoluble are in particular polymers having a solubility in water of less than 0.1% by weight.
  • a dispersion in the sense of the present invention in accordance with textbook knowledge, denotes a mixture of at least two immiscible phases, one of the at least two phases being liquid.
  • dispersions are subdivided into aerosols, emulsions and suspensions, the second or further phase being gaseous in the case of aerosols, solid in the case of emulsions and solid in the case of suspensions.
  • suspensions are preferably used in the process according to the invention.
  • the According to the invention preferably used colloidal polymer dispersions are also referred to in the art as latex.
  • the colloidal polymer dispersions used according to the invention can be prepared by all processes known to the person skilled in the art for this purpose.
  • the colloidal dispersions are prepared by emulsion polymerization of suitable monomers to give the corresponding latices.
  • the latex obtained by emulsion polymerization is used directly in the process of the invention without further workup.
  • so-called secondary dispersions can also be used as colloidal polymer dispersions.
  • These are prepared from already prepared polymers by dispersing in an aqueous medium. In this way, for example, dispersions of polyolefins such as polyethylene or polyesters can be prepared.
  • Suitable, substantially water-insoluble polymers are known to the person skilled in the art, for example, it is possible to use essentially water-insoluble polymers from the abovementioned groups.
  • Preferred substantially water-insoluble polymers are, for example, selected from the group consisting of homopolymers and copolymers of aromatic vinyl compounds, homo- and copolymers of alkyl acrylates, homopolymers and copolymers of alkyl methacrylates, homopolymers and copolymers of ⁇ -olefins, Homo- and copolymers of aliphatic dienes, homo- and copolymers of vinyl halides, homo- and copolymers of vinyl acetates, homo- and copolymers of acrylonitriles, homo- and copolymers of urethanes, homo- and copolymers of vinyl amides and copolymers composed of two or more of the abovementioned polymers forming monomer units and mixtures of the abovementioned homo- and copolymers.
  • Suitable homo- and copolymers of aromatic vinyl compounds are homo- and copolymers based on poly (alkyl) styrenes, for example polystyrene, poly- ⁇ -methylstyrene, styrene / alkyl acrylate copolymers, in particular styrene / n-butyl acrylate copolymers, styrene / alkyl methacrylate Copolymers, Acrylonitrile / Styrene / Acrylic Ester Copolymers (ASA), Styrene / Acrylonitrile Copolymers (SAN), Acrylonitrile / Butadiene / Styrene Copolymers (ABS), Styrene / Butadiene Copolymers (SB).
  • poly (alkyl) styrenes for example polystyrene, poly- ⁇ -methylstyrene, styrene / alkyl acrylate copo
  • Suitable polyalkyl acrylates are, for example, polyalkyl acrylates based on iso-butyl acrylate, tert-butyl acrylate and / or ethyl acrylate. If copolymers are used which contain polyalkyl acrylates, furthermore, methyl acrylate, 2-hydroxyethyl acrylate, hydroxypropyl acrylate and n-butyl acrylate are suitable as monomers.
  • Suitable poly (alkyl) methacrylates are, for example, polyalkyl methacrylates based on n-butyl methacrylate, isobutyl methacrylate, tert-butyl methacrylate, ethylhexyl methacrylate, glycidyl methacrylate. dylmethacrylate, methyl methacrylate, n-propyl methacrylate, iso-propyl methacrylate and / or n-pentyl methacrylate. Further, when copolymers containing poly (alkyl) methacrylates are used, hydroxypropyl methacrylate is suitable.
  • Suitable homopolymers and copolymers of .alpha.-olefins are, for example, polyethylene, polypropylene, poly (ethylene / propylene) (EPDM) and also olefin / vinyl acetate copolymers, for example ethylene / vinyl acetate copolymers and olefin / acrylate copolymers, for example ethylene glycol. len / acrylate copolymers.
  • Suitable homopolymers and copolymers of vinyl halides are, for example, polyvinyl chloride, polytrichlorethylene, polytrifluoroethylene and / or polyvinyl fluoride.
  • Suitable homopolymers and copolymers are furthermore homopolymers and copolymers based on melamine-containing compounds, 1,3-butadiene, isoprene or vinyl alcohols (insofar as they are essentially water-insoluble).
  • copolymers of acrylates, methacrylates, vinyl alcohols, polyalcohols and / or vinylaromatics with acrylic acid, maleic acid, fumaric acid, methacrylic acid and / or itaconic acid can be used (provided they are essentially water-insoluble).
  • the at least one substantially water-insoluble polymer is selected from the group consisting of polystyrene, poly- ⁇ -methylstyrene, styrene / alkyl acrylate copolymers, in particular styrene / n-butyl acrylate copolymers, styrene / alkyl methacrylate copolymers, ⁇ Methylstyrene / alkyl acrylate copolymers, ⁇ -
  • Methylstyrene / alkyl methacrylate copolymers poly (alkyl) methacrylates, polyethylene, ethylene / vinyl acetate copolymers, ethylene / acrylate copolymers, polyvinyl chloride, polyalkyl nitrile and polyvinyl acetate, polyurethanes, styrene / butadiene copolymers and styrene / acrylonitrile / butadiene copolymers.
  • the at least one substantially water-insoluble polymer selected from styrene / alkyl acrylate copolymers, in particular styrene / n-butyl acrylate copolymers and styrene / alkyl methacrylate copolymers.
  • Suitable alkyl acrylates used in the styrene / alkyl acrylate copolymers are, for example, n-butyl acrylate, iso-butyl acrylate, tert-butyl acrylate, ethyl acrylate, 2-ethylhexyl acrylate, n-hexyl acrylate, 2-hydroxyethyl acrylate, hydroxypropyl acrylate, lauryl acrylate, methyl acrylate and n-propyl acrylate wherein n-butyl acrylate, ethyl acrylate, methyl acrylate and 2-ethylhexyl acrylate are preferred.
  • Suitable alkyl methacrylates used in the styrene / alkyl methacrylate copolymers are, for example, n-butyl methacrylate, isobutyl methacrylate, tert-butyl methacrylate, ethylhexyl methacrylate, glycidyl methacrylate, hydroxymethacrylate, hydroxypropyl methacrylate, n-butyl methacrylate.
  • Propyl acrylate, iso-propyl acrylate and n-pentyl methacrylate preferably n-butyl methacrylate, ethylhexyl methacrylate and methyl methacrylate.
  • the proportion of the various monomer units in the abovementioned copolymers is preferably ri a be l.
  • the proportion of styrene in the copolymers is generally from 30 to 100% by weight, preferably from 40 to 95% by weight.
  • the aqueous medium in which the substantially water-insoluble polymer is present is generally water.
  • the aqueous medium may contain, in addition to water, the polymer A and optionally at least one amphiphilic protein further additives, for example additives which are used in the emulsion polymerization of suitable monomers for the preparation of a latex.
  • suitable additives are known to the person skilled in the art, examples of suitable additives and suitable additives being the additives and additives mentioned above with regard to the electrospinning of a polymer solution.
  • the average weight-average particle diameter of the at least one essentially water-insoluble polymer generally being from 1 nm to 2.5 ⁇ m, preferably from 10 nm to 1.2 ⁇ m, particularly preferably from 15 nm to 1 micron.
  • the average weight-average particle diameter of latex particles prepared by emulsion polymerization which in a preferred embodiment can be used in the process according to the invention, is generally from 30 nm to 2.5 ⁇ m, preferably from 50 nm to 1.2 ⁇ m (determined according to W. Scholtan and H Long in Colloid Z.
  • the colloidal suspension preferably used according to the invention may have particles with monomodal particle size distribution of the polymer particles or with bimodal or polymodal particle size distribution.
  • mono-, bi- and polymodal particle size distribution are known to the person skilled in the art.
  • the latex particles can be arranged in any manner known to the person skilled in the art. For example, only particles with gradient structure, core-shell structure, salami structure, multi-core structure, multi-layer structure and raspberry morphology are mentioned.
  • latex also means the mixture of two or more latices. The preparation of the mixture can be carried out by any known method, for example by mixing two latices at any time prior to spinning.
  • the colloidal dispersion in addition to the at least one water-insoluble polymer A and optionally at least one amphiphilic protein, additionally contains at least one water-soluble polymer B, a water-soluble polymer in the sense of the present invention being a polymer having a solubility in water of at least 0.1 wt .-% is understood.
  • the at least one water-soluble polymer B which is preferably additionally present in the colloidal dispersions, can serve as a template polymer.
  • the template polymer serves as a kind of "thickener” for the essentially water-insoluble polymers of the colloidal dispersion.
  • the water-soluble polymer B is generally removed, for example by washing / extraction with water.
  • water-insoluble polymer fibers in particular nano- or mesofibres or textile fabrics, are obtained, without disintegration of the polymer fibers.
  • the water-soluble polymer B may be a homopolymer, copolymer, block copolymer, graft copolymer, star polymer, highly branched polymer, dendrimer or a mixture of two or more of the foregoing types of polymers. According to the findings of the present invention, the addition of at least one water-soluble polymer not only accelerates / promotes fiber formation. Rather, the quality of the resulting fibers is significantly improved.
  • the water-soluble polymers B known to one skilled in the art may be added to the colloidal dispersion of at least one essentially water-insoluble polymer A in an aqueous medium and optionally at least one amphiphilic protein, in particular with polyvinyl alcohol, polyvinylformamide, polyvinylamine, polycarboxylic acid (polyacrylic acid, Polymethacrylic acid), polyacrylamide, polyitaconic acid, poly (2-hydroxyethyl acrylate), poly (N-isopropylacrylamide), polysulfonic acid (poly (2-acrylamido-2-methyl-1-propanesulfonic acid) or PAMPS), polymethacrylamide, polyalkylene oxides, for Example, polyethylene oxides; Poly-N-vinylpyrrolidone; hydroxymethyl celluloses, hydroxyethylcelluloses; Hydroxypropylcelluloses, carboxymethylcelluloses; maleic; alginates; collagens; Gelatin; Poly (ethyleneimine), polyst
  • the water-soluble polymer B is selected from polyvinyl alcohol, polyethylene oxides, polyvinylformamide, polyvinylamine and poly-N-vinylpyrrolidone.
  • the at least one water-soluble polymer B is generally in an amount of 0 to 25 wt .-%, preferably 0.5 to 20 wt .-%, particularly preferably 1 to 15 wt .-%, based on the at least one water-insoluble polymer A used.
  • the solids content of the colloidal dispersion to be used in a preferred embodiment of the invention is preferably from 5 to 60% by weight, particularly preferably from 10 to 50% by weight and very particularly preferably from 10 to 40% by weight, based on the total weight of the dispersion.
  • the electrospinning process is carried out in the preferred embodiment, when a colloidal dispersion of at least one substantially water-insoluble polymer A is electrostatically spun in an aqueous medium, generally at a temperature of 5 to 90 0 C.
  • the electrospinning process preferably takes place when using a colloidal dispersion at a temperature of from 10 to 70 ° C., more preferably from 15 to 50 ° C.
  • the process temperature depends, inter alia, on the essentially water-insoluble polymer A.
  • the colloidal dispersion used according to one embodiment of the present invention may be electrospun in any manner known to those skilled in the art, for example by extrusion of the dispersion, preferably latex, usually under low pressure through a cannula connected to one pole of a voltage source at a distance from the cannula exit arranged counter electrode.
  • the inner diameter of the cannula is 50 to 500 ⁇ m.
  • variants 1 and 2 are the embodiments referred to below as variants 1 and 2:
  • Variant 1 In electrospinning (electrostatic spinning), the solution to be formulated, colloidal dispersion or melt in an electric field with the strength of generally between 0.01 to 10 kV / cm, preferably between 1 and 6 kV / cm, and particularly preferred between 2 and 4 kV / cm, by squeezing it from one or more cannulas under low pressure. As soon as the electrical forces exceed the surface tension of the drops at the cannula tip (s), the mass transport takes place in the form of a jet on the opposite electrode. The optionally present solvent evaporates in the interelectrode space and the solid of the formulation is then present as fibers on the counter electrode. Spinning can be done in both vertical directions (bottom to top and top to bottom) and in horizontal direction.
  • Variant 2 Another preferred embodiment of the electrospinning process is a cylinder-based plant, e.g. Nanospider of the company Elmarco (Czech Rep.).
  • the solution, dispersion or melt used is in a container in which a metal roller rotates permanently or the spin formulation is metered onto the roller with a separate device.
  • the roller can be smooth, structured or provided with metal wires. In this case, part of the formulation is resistant to the roll surface.
  • the electric field between the roller and the counterelectrode (above the roller) causes the formulation to form liquid jets first, which then lose solvent or solidify the melt on the way to the counterelectrode.
  • the desired nanofiber fleece (fabric) is formed on a substrate (e.g., polypropylene, polyester, or cellulose) that passes between the two electrodes.
  • the electric field generally has the strength specified in Variant 1. Particularly preferably, in the example case in variant 2, the electric field has a strength of about 2.1 kV / cm (82 kV at 25 cm electrode spacing). Spinning can be done in both vertical directions (bottom to top and top to bottom) and in horizontal direction.
  • the process temperature means, irrespective of the electrospinning process carried out (in solution, in the melt or in a colloidal dispersion), the ambient temperature during the electrospinning process between the spin source and the counterelectrode.
  • the spinning source may be, for example, a cannula (for example a needle) or a roller in the electrospinning process.
  • Other suitable spin sources are mentioned in the above-mentioned documents concerning various electrospinning processes.
  • the stability of a fiber layer (textile fabric) formed by the fibers can be further improved, in particular with regard to water and temperature resistance. Suitable crosslinking methods and chemical intermediates are known to those skilled in the art.
  • amphiphilic proteins are used to adjust the hydrophilicity or hydrophobicity of the nano- or mesofibres or textile fabrics produced according to the method of the invention.
  • amphiphilic proteins may be incorporated directly into the nano- or mesofibers or into the fabrics during electrostatic spinning in step (i) of the process of the invention by containing the solution of polymer A, the melt of polymer A or the aqueous colloidal dispersion the polymer A are added and spun directly with electrostatic.
  • the at least one amphiphilic protein in an amount of generally 0.1 to 50 wt .-%, preferably 0.5 to 20 wt .-% , Particularly preferably 2 to 10 wt .-%, based on the at least one polymer A used.
  • the amphiphilic protein is added by mixing the amphiphilic protein with the polymer A and optionally further components such as the abovementioned additives and additives or, if a colloidal dispersion of at least one substantially water-insoluble polymer A is used in an aqueous medium, optionally at least one water-soluble one Polymer B.
  • the direct electrostatic spinning of the at least one amphiphilic protein with the at least one polymer A results in the incorporation of the amphiphilic proteins into the nanofibers or mesofibres or into the textile fabrics formed therefrom. It was found that the incorporation of the amphiphilic proteins has no significant influence on the fiber morphology (shape and diameter of the fibers). By incorporating the amphiphilic proteins, a significant influence on the hydrophilicity or hydrophobicity of the polymer A is achieved. This is reflected in a change in the contact angle towards nano- or mesofibres or textile fabrics produced therefrom which have not been treated with an amphiphilic protein.
  • the contact angles are measured according to the present application with deionized water at 23 ° C. For this purpose, about 3 ⁇ l large drops are placed on the surfaces of the fabric or the nano- or mesofibres, and with an optical contour analysis system, the contact angles formed at 5 points per pattern are determined.
  • the contact angle measurements are carried out using a DSA-10-MK2 apparatus from Krüss GmbH (Germany) and using Software Drop Shape Analysis v. 1.80.1.2. evaluated.
  • the incorporation of the amphiphilic proteins achieves a hydrophobization of the nano- or mesofibers formed from the polymers A or the textile fabrics produced therefrom.
  • the amphiphilic protein is electrostatically directly spun together with the at least one polymer A in step (i) of the process according to the invention
  • a subsequent treatment of the nano produced according to the electrostatic spin process in step (i) or mesofibers or the textile fabrics formed therefrom are treated with a solution of at least one amphiphilic protein.
  • the solution of the amphiphilic proteins may be an organic or aqueous solution, depending on the polymers to be treated or the dissolution properties of the proteins used.
  • the treatment of the nano- or mesofibers or the fabric with the solution of the amphiphilic proteins at temperatures of generally from 4 to 100 0 C, preferably 30 to 90 0 C, most preferably at 60 to 80 0 C.
  • amphiphilic proteins Following treatment of the nano- or mesofibres or fabrics with the solution of amphiphilic proteins, the solvent is removed and the nano- or mesofibers or fabrics can then be dried. Suitable amphiphilic proteins
  • Suitable amphiphilic proteins are preferably selected from amphiphilic self-assembling proteins and hydrophobins.
  • Hydrophobins are small proteins of about 100 to 150 amino acids, which occur, for example, in filamentous fungi such as Schizophyllum commune. They usually have 8 cysteine units in the molecule. Hydrophobins can be isolated from natural sources, but they can also be obtained by means of genetic engineering, as disclosed, for example, in WO 2006/082251, WO 2006/131564 or WO 2006/131478.
  • hydrophobins As emulsifiers, thickeners, surface-active substances, for hydrophilizing hydrophobic surfaces, for improving the water resistance of hydrophilic substrates, for producing oil-in-water emulsions or for oil-in-oil emulsions. Emulsions.
  • EP-A 1 252 516 discloses the coating of various substrates with a hydrophobin-containing solution at a temperature of 30 to 80 0 C. Furthermore, the use of hydrophobins as demulsifier (WO 2006/103251), inhibitors as evaporation (WO was 2006, for example / 128877) or pollution inhibitor (WO 2006/103215) have already been proposed.
  • WO 2006/131478 discloses a process for coating fibrous substrates selected from textile substrates and leather using at least one hydrophobin.
  • hydrophobins are to be understood below to mean polypeptides of the general structural formula (I)
  • X is selected for each of the 20 naturally occurring amino acids (Phe, Leu, Ser, Tyr, Cys, Trp, Pro, His, GIn, Arg, Ne Met, Thr, Asn, Lys, VaI, Ala, Asp, Glu, GIy) can stand.
  • the radicals X may be the same or different.
  • the indices standing at X each represent the number of amino acids in the respective subsequence X
  • C stands for cysteine, alanine, serine, glycine, methionine or threonine, at least four of the radicals named C being cysteine
  • the indices n and m independently represent natural numbers between 0 and 500, preferably between 15 and 300.
  • polypeptides according to the formula (I) are further characterized by the property that at room temperature after coating a glass surface, they increase the contact angle of a water droplet of at least 20 °, preferably at least 25 ° and particularly preferably 30 °, in each case compared with the contact angle an equally large drop of water with the uncoated glass surface.
  • the amino acids designated C 1 to C 8 are preferably cysteines. However, they can also be replaced by other amino acids of similar space filling, preferably by alanine, serine, threonine, methionine or glycine. However, at least four, preferably at least 5, more preferably at least 6 and in particular at least 7, of the positions C 1 to C 8 should consist of cysteines. Cysteines can either be reduced in the proteins according to the invention or form disulfide bridges with one another. Particularly preferred is the intramolecular formation of CC bridges, in particular those with at least one, preferably 2, more preferably 3 and most preferably 4 intramolecular disulfide bridges. In the exchange of cysteines described above by amino acids of similar space filling, it is advantageous to exchange in pairs those C positions which are capable of forming intramolecular disulfide bridges with one another.
  • cysteines, serines, alanines, glycines, methionines or threonines are also used in the positions marked X, the numbering of the individual C positions in the general formulas may change accordingly.
  • X, C and the indices standing at X and C have the above meaning
  • the indices n and m are numbers between 0 and 350, preferably 15 to 300
  • the proteins further by the above-mentioned Distinguish contact angle change and it is still at least 6 of the radicals named C is cysteine. Most preferably, all of the C radicals are cysteine.
  • the proteins are further characterized by the abovementioned contact angle change, and at least 6 of the C named residues are cysteine. Most preferably, all of the C radicals are cysteine.
  • the radicals X n and X m may be peptide sequences that are naturally also linked to a hydrophobin. However, one or both of the residues may be peptide sequences that are not naturally linked to a hydrophobin. Including such radicals X N and / or X m are to be understood, in which a naturally occurring in a hydrophobin peptide sequence is extended by a non-naturally occurring in a hydrophobin peptide sequence.
  • X n and / or X m are naturally non-hydrophobin-linked peptide sequences, such sequences are generally at least 20, preferably at least 35 amino acids long. They may, for example, be sequences from 20 to 500, preferably 30 to 400 and particularly preferably 35 to 100 amino acids. Such a residue, which is not naturally linked to a hydrophobin, will also be referred to below as a fusion partner.
  • the proteins may consist of at least one hydrophobin part and one fusion partner part which in nature do not coexist in this form. Fusion hydrophobins from fusion partner and hydrophobin part are described, for example, in WO 2006/082251, WO 2006/082253 and WO 2006/131564.
  • the fusion partner portion can be selected from a variety of proteins. Only a single fusion partner can be linked to the hydrophobin moiety, or several fusion partners can also be linked to a hydrophobin moiety, for example at the amino terminus (X n ) and at the carboxy terminus (X m ) of the hydrophobin moiety. However, it is also possible, for example, to link two fusion partners with a position (X n or X m ) of the protein according to the invention.
  • fusion partners are proteins which occur naturally in microorganisms, in particular in Escherischia coli or Bacillus subtilis.
  • fusion partners are the sequences yaad (SEQ ID NO: 16 in WO 2006/082251), yaae (SEQ ID NO: 18 in WO 2006/082251), ubiquitin and thioredoxin.
  • fragments or derivatives of said sequences which comprise only a part, for example 70 to 99%, preferably 5 to 50%, and particularly preferably 10 to 40% of said sequences, or in which individual amino acids or nucleotides are opposite the said sequence are changed, wherein the percentages in each case refers to the number of amino acids.
  • the fusion hydrophobin in addition to said fusion partner as one of the groups X n or X n , or as a terminal component of such a group on a so-called affinity domain (affinity tag / affinity tail) on.
  • affinity domains affinity tag / affinity tail
  • anchor groups which can interact with certain complementary groups and can serve the easier workup and purification of the proteins.
  • affinity domains have (His) k , (Arg) k , (Asp) k , (Phe) k or (Cys) k groups, k generally being a natural number from 1 to 10. It may preferably be a (His) k group, where k is 4 to 6.
  • the group X n and / or m X may consist exclusively of such an affinity domain or a naturally or not naturally have a hydrophobicity linked radical X n and X m is extended by a terminal affinity domain.
  • hydrophobins used according to the invention may also be modified in their polypeptide sequence, for example by glycosylation, acetylation or else by chemical crosslinking, for example with glutaraldehyde.
  • hydrophobins for practicing the present invention are the dewA, rodA, hypA, hypB, sc3, basfl, basf2 hydrophobins. These hydrophobins including their sequences are disclosed, for example, in WO 2006/082251. Unless stated otherwise, the sequences given below refer to the sequences disclosed in WO 2006/082,251. An overview table with the SEQ ID numbers can be found in WO 2006/082 251 on page 20.
  • fusion proteins yaad-Xa-dewA-his SEQ ID NO: 20
  • yaad-Xa-rodA-his SEQ ID NO: 22
  • yaad-Xa-basfl-his SEQ ID NO: 24
  • polypeptide sequences given in parentheses and the nucleic acid sequences coding therefor, in particular the sequences according to SEQ ID NO: 19, 21, 23.
  • yaad-Xa-dewA-his SEQ ID NO: 20
  • SEQ ID NO: 20 can be used.
  • proteins which, starting from the amino acid sequences shown in SEQ ID NO. 20, 22 or 24 shown by exchange, insertion or deletion of at least one, up to 10, preferably 5, more preferably 5% of all amino acids, and still have the biological property of the starting proteins at least 50%, are particularly preferred embodiments.
  • the biological property of the proteins is hereby understood as the change in the contact angle already described by at least 20 °.
  • Particularly suitable derivatives for carrying out the present invention are from yaad-XadewA-his (SEQ ID NO: 20), yaad-Xa-rodA-his (SEQ ID NO: 22) or yaad-Xa-basfl-his (SEQ ID NO: 24) derivatives derived from truncation of the yaad fusion partner.
  • yaad-XadewA-his SEQ ID NO: 20
  • yaad-Xa-rodA-his SEQ ID NO: 22
  • yaad-Xa-basfl-his SEQ ID NO: 24
  • the truncated residue should comprise at least 20, preferably at least 35, amino acids.
  • a truncated radical having 20 to 293, preferably 25 to 250, particularly preferably 35 to 150 and for example 35 to 100 amino acids can be used.
  • An example of such a protein is yaad40-Xa-dewA-his (SEQ ID NO: 26 in PCT / EP2006 / 064720), which has a 40 amino acid truncated yaad residue.
  • a cleavage site between the hydrophobin and the fusion partner or the fusion partners can be used to cleave off the fusion partner and release the pure hydrophobin in underivatized form (for example by BrCN cleavage to methionine, factor Xa, enterokinase, thrombin, TEV cleavage Etc.).
  • hydrophobins used in the invention can be prepared chemically by known methods of peptide synthesis, such as by Merrifield solid phase synthesis.
  • Naturally occurring hydrophobins can be isolated from natural sources by suitable methods. As an example, let Wösten et. al., Eur. J. Cell. Bio. 63, 122-129 (1994) or WO 1996/41882. A genetic engineering preparation for hydrophobins without fusion partner from Talaromyces thermophilus is described by US 2006/0040349.
  • fusion proteins can preferably be carried out by genetic engineering methods in which a nucleic acid sequence coding for the fusion partner and a hydrophobin part, in particular DNA sequence, are combined in such a way that the desired protein is produced in a host organism by gene expression of the combined nucleic acid sequence.
  • a production method for example, is disclosed by WO 2006/082251 or WO 2006/082253.
  • the fusion partners greatly facilitate the production of hydrophobins. Fusion hydrophobins are produced in genetically engineered processes with significantly better yields than hydrophobins without fusion partners.
  • the fusion hydrophobins produced by the host organisms according to the genetic engineering process can be worked up in a manner known in principle and purified by known chromatographic methods.
  • the simplified work-up and purification process disclosed in WO 2006/082253, pages 1 1/12 can be used.
  • the fermented cells are first separated from the fermentation broth, digested and the cell debris of the inclusion bodies (inclusion bodies) separated.
  • inclusion bodies for example by acids, bases and / or detergents can be digested in a manner known in principle in order to release the fusion hydrophobins.
  • the inclusion bodies with the fusion hydrophobins used according to the invention can generally be completely dissolved within about 1 h already using 0.1 M NaOH.
  • the solutions obtained can - if necessary after setting the desired pH - are used without further purification for carrying out this invention.
  • the fusion hydrophobins can also be isolated from the solutions as a solid.
  • the isolation can preferably be effected by means of spray granulation or spray drying, as described in WO 2006/082253, page 12.
  • the products obtained by the simplified work-up and purification process, apart from residues of cell debris, usually comprise about 80 to 90% by weight of proteins.
  • the amount of fusion hydrophobins is generally from 30 to 80% by weight relative to the amount of all proteins.
  • the isolated products containing fusion hydrophobins can be stored as solids and dissolved for use in the respective desired media.
  • the fusion hydrophobins can be used as "pure" hydrophobins for the practice of this invention. Cleavage is advantageously carried out after isolation of the inclusion bodies and their dissolution.
  • amphiphilic proteins which can be used in the method according to the invention are amphiphilic self-assembling proteins.
  • Amphiphilic, self-assembling proteins are composed of polypeptides composed of amino acids, in particular of the 20 naturally occurring amino acids.
  • the amino acids may also be modified, for example, acetylated, glycosylated, farnesylated. It is suitable to use phage inhibiting protein e, e.g. C16 spider silk proteins are disclosed in WO 2007/082936.
  • the amphiphilic self-assembling proteins are spider silk proteins.
  • the spider silk proteins could be isolated in their original form from spiders.
  • suitable proteins are silk proteins that could be isolated from the spider's "major ampullate” gland
  • Preferred silk proteins are ADF3 and ADF4 from the "Araneus diadematus” major ampullate gland (Guerette et al., Science 272, 5258: 112-5 (1996)).
  • Equally suitable proteins for use in the method according to the invention are natural or synthetic proteins which are derived from natural silk proteins and which have been produced heterologously in prokaryotic or eukaryotic expression systems using genetic engineering working methods.
  • prokaryotic expression organisms are Escherichia coli, Bacillus subtilis, Bacillus megaterium, Corynebacterium glutamicum and others.
  • Nonlimiting examples of eukaryotic expression organisms are yeasts such as Saccharomyces cerevisiae, Pichia pastoris and other filamentous fungi such as Aspergillus niger, Aspergillus oryzae, Aspergillus nidulans, Trichoderma reesei, Acremonium chrysogenum and other mammalian cells such as Heia cells, COS cells, CHO cells and others, insect cells such as Sf9 cells, MeL cells and others.
  • yeasts such as Saccharomyces cerevisiae, Pichia pastoris and other filamentous fungi such as Aspergillus niger, Aspergillus oryzae, Aspergillus nidulans, Trichoderma reesei, Acremonium chrysogenum and other mammalian cells such as Heia cells, COS cells, CHO cells and others, insect cells such as Sf9 cells, MeL cells and others.
  • Synthetic proteins which are based on repeating units of natural silk proteins are particularly preferably used in the process according to the invention.
  • these may additionally contain one or more natural non-repetitive silk protein sequences (Winkler and Kaplan, J. Biotechnol., 74: 85-93 (2000)).
  • synthetic spider silk proteins based on repeating units of natural spider silk proteins are preferred.
  • synthetic repetitive spider silk protein sequences these may additionally contain one or more natural non-repetitive spider silk protein sequences.
  • C16 protein (Hümmerich et al., Biochemistry, 43 (42): 13604-13612 (2004)).
  • This protein has the polypeptide sequence shown in SEQ ID NO: 1 in WO 2007/082936.
  • functional equivalents, functional derivatives and salts of this sequence are also preferred.
  • Functional equivalents, functional derivatives and salts of this sequence are to be understood as meaning the functional equivalents, functional derivatives and salts as defined in WO 2007/082936.
  • amphiphilic self-assembling proteins are disclosed in unpublished prior PCT application Serial No. PCT / EP2008 / 057526 (date of application: June 16, 2008). Particularly suitable synthetic reactive proteins are described below, with the S16 and R16 proteins being particularly preferred.
  • N is a natural integer with 2 ⁇ n ⁇ 12.
  • Repetitive proteins according to the present application are characterized in that at least 60%, preferably at least 80% of their amino acid sequence consists of repeating units.
  • a repeat unit is an amino acid sequence of 7-100, preferably 12-60, and more preferably 1-5 amino acids in length, within a protein several times as an identical sequence or as a variation of 70%, preferably at least 80%, and most preferably at least 90% identity occurs.
  • Repetitive proteins according to the present invention may contain identical copies or variations of a single or multiple different amino acid sequences.
  • the repeating units may be linked by linkers which preferably contain 1 to 30 amino acids, more preferably 1 to 20 amino acids.
  • the amino acid sequence of a linker can be derived from other proteins, preferably structural proteins, or have no natural role model or be completely absent.
  • any number of repeat units preferably 1-100, more preferably, 1-0-65, and most preferably 15-35, may be joined together.
  • consensus sequence refers to an amino acid sequence that frequently contains amino acids occurring at a particular position, other amino acids being unspecified but replaced by the wild-type X term instead of the commonly used one-letter code for amino acids.
  • the one-letter code for amino acids used herein is known to those skilled in the art.
  • the ratio of the number of consensus sequences (I) to the number of consensus sequences (II) within 60%, preferably at least 80% of the repeat units of the repetitive protein is less than five and greater than two.
  • the ratio of the number of consensus sequences (I) to the number of consensus sequences (II) within 60%, preferably at least 80% of the repeat units of the repetitive protein is equal to or less than two and greater than one, preferably two.
  • the ratio of the number of consensus sequences (I) to the number of consensus sequences (II) within 60%, preferably at least 80% of the repeat units of the repetitive protein is equal to or less than one, preferably equal to one. In one embodiment, 60%, preferably at least 80% of the repeating units of the repetitive protein contain the partial sequence GGRPSDTYG or GGRPSSSYG.
  • the repetitive proteins contain the repeat units PGSSAAAAAAASGPGQGQGQGQGQGGRPSDTYG or SAAAAAAAGPGGGNGGRPSDTYGAPGGGNGGRPSSSYG.
  • the repetitive protein according to the invention contains amino terminal or carboxy terminal a peptide sequence of 4-30 and particularly preferably 5-15 amino acids in length, which serves to detect the protein by immunoblotting or to purify the protein via affinity chromatography.
  • peptide sequences are 6xHis tag (HHHHHH), T7 tag (MASMTGGQQMG), S-tag (KETAAAKFERQHMDS), c-Myc tag (EQKLISEEDL), Strep tag (WSHPQFEK), or HA tag (YPYDVPDYA ) (Terpe, Appl Microbiol Biotechnol; 60 (5): 523-33 (2003)).
  • Amino acid sequences may be inserted between the protein according to the invention and the additional peptide sequence, which allow the chemical or enzymatic cleavage of the peptide sequence.
  • amino acid sequence of the repetitive protein of SEQ ID NO 2 or parts of this sequence corresponds.
  • amino acid sequence of the repetitive protein of SEQ ID NO 4 or parts of this sequence corresponds.
  • repetitive proteins can be carried out by expression of natural gene sequences which have been molecular-biologically modified in order to obtain the structure according to the invention. Methods for the isolation and modification of natural gene sequences are known to the person skilled in the art.
  • the production of the repetitive proteins preferably takes place by expression of synthetically produced gene sequences.
  • One way of producing synthetic gene sequences is in Huemmerich et al., Biochemistry. 43 (42): 13604-12, (2004).
  • Preferred nucleic acid sequences are SEQ ID NO 1 and SEQ ID NO 3.
  • Non-limiting examples of prokaryotic expression organisms are Escherichia coli, Bacillus subtilis, Bacillus megaterium, Cory- nebacterium glutamicum and others.
  • Nonlimiting examples of eukaryotic expression organisms are yeasts such as Saccharomyces cerevisiae, Pichia pastoris and others, filamentous fungi such as Aspergillus niger, Aspergillus oryzae, Aspergillus nidulans, Trichoderma reesei, Acremonium chrysogenum and others, mammalian cells such as Heia cells, COS cells, CHO Cells, among others, insect cells such as Sf9 cells, MEL cells, among others, plants or plant cells such as Solanum tuberosum, Nicotiana et al.
  • yeasts such as Saccharomyces cerevisiae, Pichia pastoris and others
  • filamentous fungi such as Aspergillus niger, Aspergillus oryzae, Aspergillus nidulans, Trichoderma reesei, Acremonium chrysogenum and others
  • mammalian cells such as He
  • the present invention relates to a process for the production of nano- or mesofibres or textile fabrics containing nano- or mesofibers, comprising the step:
  • Suitable essentially water-insoluble polymers A and suitable electrostatic spin processes for spinning a colloidal dispersion of at least one essentially water-insoluble polymer A in an aqueous medium suitable amphiphilic, self-assembling proteins, suitable hydrophobins and a suitable process for electrostatic spinning in the presence of at least one amphiphilic protein are described above called.
  • nano- or mesofibers can be obtained or directly textile fabrics containing nano- or mesofibres. Suitable processes for the production of the textile fabrics and the nano- or mesofibers are mentioned above.
  • a further subject of the present invention therefore relates to nano- or mesofibres obtainable by the process according to the invention and to textile fabrics obtainable by the process according to the invention.
  • the nano- or mesofibres or the textile fabrics are characterized in that their hydrophobicity or hydrophilicity can be adjusted in a targeted manner by the amphiphilic protein present.
  • the diameter of the nano- or mesofibers according to the invention is preferably 10 nm to 50 ⁇ m, particularly preferably 50 nm to 2 ⁇ m and very particularly preferably 100 nm to 1 ⁇ m.
  • the length of the fibers depends on the purpose and is usually 50 microns to several kilometers.
  • the textile fabrics according to the invention can be produced directly in the electrospinning process, for example by forming the polymer threads formed in the electrospinning process on a treadmill to form a nonwoven layer be filed.
  • the nano- or mesofibres formed according to the electrospinning process according to the invention can be subsequently woven into textile fabrics.
  • the textile fabrics can be constructed exclusively from the nano- or mesofibers according to the invention.
  • the textile fabrics may contain conventional fibers known to the person skilled in the art.
  • the textile fabric according to the invention is constructed from conventional fibers and has a support (layer) which contains the polymer fibers according to the invention. It is furthermore possible, for example, for the textile fabric to be constructed from a mixture of conventional fibers and nano- or mesofibers according to the invention.
  • amphiphilic proteins according to the invention during the production process of the textile fabrics or by treatment of the textile fabrics or nano- or mesofibers according to the invention with the at least one amphiphilic protein results in a change in contact angle relative to the corresponding untreated textile fabrics or nano- or mesofibers or in Absence of amphiphilic proteins produced fabric or nano or mesofibers of generally at least +/- 10 °, preferably at least +/- 20 °, more preferably at least +/- 30 ° reached.
  • a contact angle change of generally at least + 10 °, preferably at least + 20 °, more preferably at least + 30 ° is achieved
  • a contact angle change of generally at least -10 °, preferably at least -20 ° is particularly preferred at least -30 °.
  • the contact angle measurements are made as described above.
  • the hydrophobicity or hydrophilicity of the fabrics constructed of nano- or mesofibers depending on the desired application.
  • the hydrophobing can provide improved soil repellency or improved filtration properties of the fibers or fabrics.
  • the textile fabrics according to the invention and the nano- or mesofibers according to the invention themselves can be used for numerous applications.
  • Preferred applications are selected from the group consisting of the use in the following applications: filters or filter parts, non-wovens, nonwovens, in particular for gas, air and / or liquid filtration, technical or household textiles or components or Coatings of such textiles as wipes, facial tissues, clothing, cleaning textiles, hygiene articles, medical textiles, etc., coatings of packaging, for example coatings of paper, for use in wound healing or as wound dressing, for the transport or release of active ingredients.
  • the nano- or mesofibers according to the invention are used in the form of the textile fabrics of the invention.
  • the nano- or mesofibers according to the invention themselves, for example as additives (fillers) for polymers or as precursors for the production of other fibers and continuous layers.
  • 161 g aqueous solution of an amphiphilic protein (batch 1: 1, 7 wt .-% aqueous solution of hydrophobin A, 2: 1, 9 wt .-% aqueous solution of hydrophobin B, batch 3: 2.9 wt. -% aqueous solution of the protein S16, batch 4: 3.5 wt .-% aqueous solution of the spider silk protein C16.
  • Hydrophobin A fusion hydrophobin with the complete fusion partner yaad: yaad-Xa-dewA-his (SEQ ID NO: 20 in WO2006 / 082 251)
  • hydrophobin B fusion hydrophobin with one on 40 amino acids shortened
  • Spider silk protein C16 SEQ ID NO: 1 in WO 2007/082936 Protein S16: SEQ ID NO: 4 in the present application (SEQ ID NO: 4 in the non-prepublished prior PCT application with the
  • Table 1 summarizes the concentrations of the individual components in the formulation used for electrospinning and in the solid.
  • a solution is prepared containing 240 g of a styrene / butyl acrylate copolymer (50: 50) in the form of an aqueous dispersion (50 wt .-%) (Acronal 290D ®) and 99 g of polyvinylformamide contains (A5 / 35) in the form a 5.05% by weight aqueous solution, wherein the polyvinylformamide has a weight average molecular weight of 3,000,000.
  • a styrene / butyl acrylate copolymer 50: 50
  • an aqueous dispersion 50 wt .-%)
  • polyvinylformamide contains (A5 / 35) in the form a 5.05% by weight aqueous solution, wherein the polyvinylformamide has a weight average molecular weight of 3,000,000.
  • Nanoturavliese are manufactured in a Nanospider Elektrospin plant of the company Elmarco (Czech Republic).
  • the working principle of the system is shown schematically in Fig. 1.
  • the dispersion used according to the batches or corresponding to the comparative batch is in a container with the dissolved proteins in which a smooth metal roller rotates permanently. In this case, part of the formulation is resistant to the roll surface.
  • the electric field between the roller and the counter electrode (above the roller) causes the formulation to form nanofibers.
  • the desired nanofiber fleece is formed on a polypropylene substrate that passes between the two electrodes.
  • the electric field is approximately 2.1 kV / cm (82 kV at 25 cm electrode spacing) in all batches and the comparative batch.
  • Fig. 1 mean: G counter electrode S substrate
  • the amphiphilic proteins hydrophobin A and hydrophobin B as well as the amphiphilic proteins S16 and C16 from aqueous solution together with the styrene / butyl acrylate copolymer are processed into nanofiber nonwovens, whereas in the comparative batch no amphiphilic protein is added , The properties of the produced nonwovens (textile fabrics) were then checked by means of contact angle analysis.
  • the contact angles are measured according to the present application with deionized water at 23 ° C. For this purpose, about 3 ⁇ l large drops are placed on the surfaces of the fabric or the nano- or mesofibres, and with an optical contour analysis system, the contact angles formed at 5 points per pattern are determined.
  • the contact angle measurements are carried out using a DSA-10-MK2 apparatus from Krüss GmbH (Germany) and using Software Drop Shape Analysis v. 1.80.1.2. evaluated.
  • a contact angle measurement in the finished nonwovens results in all the webs according to the invention resulting from the formulations (1 to 4) their significant hydrophobization, which is shown in Table 2. Furthermore, there is a delayed sinking in of water drops which are deposited on the nonwoven surface.
  • Tab. 2 Contact angle measurement of water droplets deposited on the fabrics made of fibers. In each case three different individual measurements were carried out and then the average values were calculated therefrom.
  • Pieces of the nonwovens according to the invention are treated with Western Blocking Reagent (Roche, 10 ⁇ conc) for 30 minutes and then washed twice with TTBS buffer (20 mM tris (hydroxymethyl) aminomethane; 150 mM NaCl, pH 7.5; , 05% polyoxyethylene (20) sorbitan monolaurate) and once with TBS buffer (20 mM Tris (hydroxymethyl) aminomethane; 150 mM NaCl, pH 7.5) for 5 minutes each.
  • Western Blocking Reagent (Roche, 10 ⁇ conc) for 30 minutes and then washed twice with TTBS buffer (20 mM tris (hydroxymethyl) aminomethane; 150 mM NaCl, pH 7.5; , 05% polyoxyethylene (20) sorbitan monolaurate) and once with TBS buffer (20 mM Tris (hydroxymethyl) aminomethane; 150 mM NaCl, pH 7.5) for 5 minutes each.
  • the incubation of the webs is carried out with an antibody directed against the existing respectively in these proteins T7 tag sequence antibody (T7-tag ® Antibody AP Conjugate, Novagen, US) to which the enzyme alkaline phosphatase is coupled and which is diluted 1: 1000 in 20 ml of TBS buffer.
  • T7 tag sequence antibody T7-tag ® Antibody AP Conjugate, Novagen, US
  • the nonwovens containing hydrophobin A and B are first incubated with an antibody directed against the His-tag sequence contained in these proteins (Monoclonal Anti HexaHis Antibody, Sigma, Germany). This is followed by the specific recognition and binding of a second enzyme-linked antibody (Anti Mouse IgG AP Antibody, Sigma, Germany) to the first antibody.
  • the batches are then washed twice with TTBS buffer and once with TBS buffer for 5 minutes each.
  • the reaction of the alkaline phosphatase coupled to the respective last antibody is started by addition of a substrate solution (NBT / BCIP system, Roche AG, Germany).
  • NBT / BCIP system Roche AG, Germany.
  • To prepare the alkaline phosphatase substrate 1 tablet of NBT / BCIP is dissolved in 50 ml of water. The reaction mixtures are then incubated until the clearly visible red-violet color and then stopped by washing away the substrate solution. The staining of the nonwovens thus allows conclusions about the enzyme activity and thus the presence of the bound antibodies.
  • the illustrated assay shows that nonwovens according to the invention have significantly stronger red-violet coloration than the identically treated comparative formulation (FIG. 2).
  • Fig. 2 Immunological detection of amphiphilic proteins in styrene / butyl acrylate nonwovens by means of specific antibodies. A red-violet dyeing of the nonwovens indicates an antibody reaction and thus the presence of the amphiphilic proteins:
  • a 4 batch 4 (C16 spider silk protein) Electron micrographs of the nonwovens produced by adding the amphiphilic proteins (according to runs 1 to 4) show no significant differences to the nonwoven prepared according to the comparative batch.
  • FIGS. 3A-D The webs according to the invention are shown in FIGS. 3A-D and the web according to the comparative example is shown in FIG. 3E.
  • 3A shows the inventive nonwoven according to approach 1
  • FIG. 3B the nonwoven according to the invention according to approach 2
  • FIG. 3C the inventive nonwoven according to approach 3
  • FIG. 3D the nonwoven according to the invention according to approach 4
  • FIG. 3E the nonwoven according to the comparative approach
  • FIG. 3 Electron micrographs of protein-containing nonwovens: In FIG. 3 A-E:
  • nonwovens produced from polymers can be subsequently modified by protein coating.
  • hydrophobic nonwovens of the impact polystyrene HiPS 495F are used.
  • Example 1 The processing of the approach to a nanofiber nonwoven fabric is carried out as described in Example 1 by electrospinning the polystyrene solution by means of Nanospider Elektrospinn plant Elmarco (Czech Republic). The following spinning parameters are applied: electrode distance 25cm, voltage: 82 kV, roller rotation speed 50 Hz, relative humidity 48%, temperature: 23 ° C.
  • Tab. 3 Contact angle measurement of water droplets, which are deposited on the fiber webs. In each case at least two different individual measurements are carried out and then the average values are calculated therefrom.
  • the detection of the proteins used in the nonwoven fabric is carried out as described in Example 1 by antibodies. The same antibodies are selected and the experiments are carried out under the conditions described in Example 1.
  • the red-violet coloration of the hydrophobin B or C16 spider silk protein-treated nonwovens clearly occurring in this experiment compared to the control batch without protein clearly shows that a surface coating of the nonwovens with the proteins has taken place (FIG. 4).
  • Fig. 4 Immunological detection of protein coating on polystyrene nonwovens by means of specific antibodies. A red-violet dyeing of the nonwovens indicates an antibody reaction and thus the presence of the amphiphilic proteins:
  • V control compound (without protein) A 1 batch 1 (hydrophobin A) A 2 batch 2 (hydrophobin B)

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  • Engineering & Computer Science (AREA)
  • Textile Engineering (AREA)
  • Chemical & Material Sciences (AREA)
  • Chemical Kinetics & Catalysis (AREA)
  • General Chemical & Material Sciences (AREA)
  • Mechanical Engineering (AREA)
  • Manufacturing & Machinery (AREA)
  • Artificial Filaments (AREA)
  • Nonwoven Fabrics (AREA)
  • Spinning Methods And Devices For Manufacturing Artificial Fibers (AREA)

Abstract

L'invention concerne un procédé de fabrication de nanofibres ou de mésofibres et/ou de produits textiles plats contenant des nanofibres ou des mésofibres, comprenant l'étape de filage électrostatique d'au moins un polymère A. Le polymère est filé en présence d'au moins une protéine amphiphile et/ou les nanofibres ou mésofibres et/ou le produit textile plat sont traités à l'aide d'au moins une protéine amphiphile. L'invention concerne en outre des nanofibres ou mésofibres pouvant être obtenues à l'aide du procédé selon l'invention, des produits textiles plats pouvant être obtenus à l'aide du procédé selon l'invention ainsi que l'utilisation des nanofibres ou mésofibres, ou encore des produits textiles plats.
PCT/EP2009/067492 2008-12-23 2009-12-18 Modification de nanofibres ou de mésofibres ou de produits textiles plats produits par électrofilage à l'aide de protéines amphiphiles WO2010072665A1 (fr)

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CN102277642A (zh) * 2011-07-04 2011-12-14 西南科技大学 一种热塑性羧甲基纤维素衍生物静电纺丝制备纤维的方法
WO2012091636A2 (fr) * 2010-12-30 2012-07-05 Федеральное Государственное Бюджетное Образовательное Учреждение Высшего Профессионального Образования "Саратовский Государственный Университет Имени Н.Г. Чернышевского" Tissu biopolymérique, composition d'une solution de formation destinée à sa préparation, procédé de préparation d'une solution de formation, tissu à usage biomédical, procédé de sa modification, pansement biologique et procédé de traitement de plaies
CN102926027A (zh) * 2012-10-31 2013-02-13 西南科技大学 静电纺丝制备改性魔芋葡甘露聚糖/生物降解聚酯共混纤维的方法
EP2615107A1 (fr) 2012-01-16 2013-07-17 Universität Bayreuth Nouveau biopolymère doté d'excellentes capacités de résistance à la traction, d'extensibilité et de durcissement
CN104480699A (zh) * 2014-12-15 2015-04-01 中国科学技术大学 光控开关控制元件的制备方法及光控开关
WO2016193547A1 (fr) 2015-06-02 2016-12-08 Teknologian Tutkimuskeskus Vtt Oy Procédé permettant d'accroître la stabilité d'une mousse
CN108385174A (zh) * 2018-04-24 2018-08-10 东华大学 一种分离控制电场多孔球形静电纺丝喷头及其纺丝方法
CN109629015A (zh) * 2018-12-28 2019-04-16 李瑞锋 一种分离控制电场多孔圆柱形静电纺丝装置及其纺丝方法
CN109944072A (zh) * 2019-03-18 2019-06-28 温州优巴信息技术有限公司 一种含双芘纳米颗粒的海藻酸钠无纺布材料及其制备方法
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WO2022033743A1 (fr) 2020-08-14 2022-02-17 Re-Organic As Procédé pour disperser de la nanocellulose dans des polymères et produits correspondants
CN116005290A (zh) * 2022-12-30 2023-04-25 华南理工大学 一种含功能蛋白的高疏水复合纳米纤维及其制备方法和应用

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WO2012091636A3 (fr) * 2010-12-30 2012-10-04 Федеральное Государственное Бюджетное Образовательное Учреждение Высшего Профессионального Образования "Саратовский Государственный Университет Имени Н.Г. Чернышевского" Tissu biopolymérique, composition d'une solution de formation destinée à sa préparation, procédé de préparation d'une solution de formation, tissu à usage biomédical, procédé de sa modification, pansement biologique et procédé de traitement de plaies
RU2468129C2 (ru) * 2010-12-30 2012-11-27 Государственное образовательное учреждение высшего профессионального образования "Саратовский государственный университет им. Н.Г. Чернышевского" Биополимерное волокно, состав формовочного раствора для его получения, способ приготовления формовочного раствора, полотно биомедицинского назначения, способ его модификации, биологическая повязка и способ лечения ран
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EP2615107A1 (fr) 2012-01-16 2013-07-17 Universität Bayreuth Nouveau biopolymère doté d'excellentes capacités de résistance à la traction, d'extensibilité et de durcissement
CN102926027A (zh) * 2012-10-31 2013-02-13 西南科技大学 静电纺丝制备改性魔芋葡甘露聚糖/生物降解聚酯共混纤维的方法
CN102926027B (zh) * 2012-10-31 2014-12-03 西南科技大学 静电纺丝制备改性魔芋葡甘露聚糖/生物降解聚酯共混纤维的方法
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WO2016193547A1 (fr) 2015-06-02 2016-12-08 Teknologian Tutkimuskeskus Vtt Oy Procédé permettant d'accroître la stabilité d'une mousse
CN108385174A (zh) * 2018-04-24 2018-08-10 东华大学 一种分离控制电场多孔球形静电纺丝喷头及其纺丝方法
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CN109944072A (zh) * 2019-03-18 2019-06-28 温州优巴信息技术有限公司 一种含双芘纳米颗粒的海藻酸钠无纺布材料及其制备方法
CN109989120A (zh) * 2019-03-18 2019-07-09 广东工业大学 一种静电纺丝双通道注射器及其实现方法
CN109989120B (zh) * 2019-03-18 2021-09-07 广东工业大学 一种静电纺丝双通道注射器及其使用方法
WO2022033743A1 (fr) 2020-08-14 2022-02-17 Re-Organic As Procédé pour disperser de la nanocellulose dans des polymères et produits correspondants
CN116005290A (zh) * 2022-12-30 2023-04-25 华南理工大学 一种含功能蛋白的高疏水复合纳米纤维及其制备方法和应用
CN116005290B (zh) * 2022-12-30 2024-04-05 华南理工大学 一种含功能蛋白的高疏水复合纳米纤维及其制备方法和应用

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