RU2545331C2 - Способ получения полимерсодержащих волокон - Google Patents

Способ получения полимерсодержащих волокон Download PDF

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Publication number: RU2545331C2
Authority: RU; Russia
Prior art keywords: seq; module; fiber; amino acid; repeating
Prior art date: 2010-03-17

Application number

RU2012144053/05A

Other languages

English (en)

Russian (ru)

Other versions

RU2012144053A (ru

Inventor

Андреас БАУШ

Себастьян РАММЕНЗЕЕ

Original Assignee

Амсилк Гмбх

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.)

2010-03-17

Filing date

2011-03-16

Publication date

2015-03-27

2011-03-16 Application filed by Амсилк Гмбх filed Critical Амсилк Гмбх

2014-04-27 Publication of RU2012144053A publication Critical patent/RU2012144053A/ru

2015-03-27 Application granted granted Critical

2015-03-27 Publication of RU2545331C2 publication Critical patent/RU2545331C2/ru

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108091033319 polynucleotide Proteins 0.000 description 1
102000040430 polynucleotide Human genes 0.000 description 1
239000002157 polynucleotide Substances 0.000 description 1
210000004896 polypeptide structure Anatomy 0.000 description 1
229920002451 polyvinyl alcohol Polymers 0.000 description 1
235000019422 polyvinyl alcohol Nutrition 0.000 description 1
230000004481 post-translational protein modification Effects 0.000 description 1
239000000843 powder Substances 0.000 description 1
239000002243 precursor Substances 0.000 description 1
150000003141 primary amines Chemical class 0.000 description 1
125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 1
238000012545 processing Methods 0.000 description 1
230000012846 protein folding Effects 0.000 description 1
230000002285 radioactive effect Effects 0.000 description 1
238000003259 recombinant expression Methods 0.000 description 1
238000011160 research Methods 0.000 description 1
239000013557 residual solvent Substances 0.000 description 1
230000000717 retained effect Effects 0.000 description 1
CDAISMWEOUEBRE-UHFFFAOYSA-N scyllo-inosotol Natural products OC1C(O)C(O)C(O)C(O)C1O CDAISMWEOUEBRE-UHFFFAOYSA-N 0.000 description 1
239000000600 sorbitol Substances 0.000 description 1
210000000130 stem cell Anatomy 0.000 description 1
239000005720 sucrose Substances 0.000 description 1
239000000725 suspension Substances 0.000 description 1
229920001059 synthetic polymer Polymers 0.000 description 1
210000002435 tendon Anatomy 0.000 description 1
229920001169 thermoplastic Polymers 0.000 description 1
239000004416 thermosoftening plastic Substances 0.000 description 1
125000003396 thiol group Chemical group [H]S* 0.000 description 1
210000002268 wool Anatomy 0.000 description 1
239000002759 woven fabric Substances 0.000 description 1

Images

Classifications

- 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
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/43504—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from invertebrates
- C07K14/43563—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from invertebrates from insects
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K7/00—Peptides having 5 to 20 amino acids in a fully defined sequence; Derivatives thereof
- C07K7/04—Linear peptides containing only normal peptide links
- C07K7/06—Linear peptides containing only normal peptide links having 5 to 11 amino acids
- 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
- 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
- D01F4/00—Monocomponent artificial filaments or the like of proteins; Manufacture thereof
- 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
- D01F6/68—Monocomponent artificial filaments or the like of synthetic polymers; Manufacture thereof from homopolycondensation products from polyaminoacids or polypeptides
- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10—TECHNICAL SUBJECTS COVERED BY FORMER USPC
- Y10T—TECHNICAL SUBJECTS COVERED BY FORMER US CLASSIFICATION
- Y10T442/00—Fabric [woven, knitted, or nonwoven textile or cloth, etc.]
- Y10T442/30—Woven fabric [i.e., woven strand or strip material]
- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10—TECHNICAL SUBJECTS COVERED BY FORMER USPC
- Y10T—TECHNICAL SUBJECTS COVERED BY FORMER US CLASSIFICATION
- Y10T442/00—Fabric [woven, knitted, or nonwoven textile or cloth, etc.]
- Y10T442/60—Nonwoven fabric [i.e., nonwoven strand or fiber material]

Landscapes

Chemical & Material Sciences (AREA)
Engineering & Computer Science (AREA)
Health & Medical Sciences (AREA)
Textile Engineering (AREA)
Organic Chemistry (AREA)
Life Sciences & Earth Sciences (AREA)
Chemical Kinetics & Catalysis (AREA)
General Chemical & Material Sciences (AREA)
Molecular Biology (AREA)
Medicinal Chemistry (AREA)
Proteomics, Peptides & Aminoacids (AREA)
Zoology (AREA)
Genetics & Genomics (AREA)
Biochemistry (AREA)
Biophysics (AREA)
General Health & Medical Sciences (AREA)
Manufacturing & Machinery (AREA)
Gastroenterology & Hepatology (AREA)
Toxicology (AREA)
Insects & Arthropods (AREA)
Tropical Medicine & Parasitology (AREA)
Mechanical Engineering (AREA)
Peptides Or Proteins (AREA)
Materials For Medical Uses (AREA)
Artificial Filaments (AREA)

RU2012144053/05A 2010-03-17 2011-03-16 Способ получения полимерсодержащих волокон RU2545331C2 (ru)

Applications Claiming Priority (3)

Application Number	Priority Date	Filing Date	Title
PCT/EP2010/001694 WO2011113446A1 (fr)	2010-03-17	2010-03-17	Procédé de fabrication de fibres contenant un polypeptide
EPPCT/EP2010/001694		2010-03-17
PCT/EP2011/001307 WO2011113592A1 (fr)	2010-03-17	2011-03-16	Procédé de fabrication de fibres contenant un polymère

Publications (2)

Publication Number	Publication Date
RU2012144053A RU2012144053A (ru)	2014-04-27
RU2545331C2 true RU2545331C2 (ru)	2015-03-27

Family

ID=43035008

Family Applications (1)

Application Number	Title	Priority Date	Filing Date
RU2012144053/05A RU2545331C2 (ru)	2010-03-17	2011-03-16	Способ получения полимерсодержащих волокон

Country Status (5)

Country	Link
US (1)	US20130172478A1 (fr)
AU (1)	AU2011229482B2 (fr)
CA (1)	CA2789647C (fr)
RU (1)	RU2545331C2 (fr)
WO (2)	WO2011113446A1 (fr)

Cited By (1)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
RU2769982C2 (ru) *	2016-04-28	2022-04-12	Спайбер Инк.	Модифицированный фиброин

Families Citing this family (29)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
US9617315B2 (en)	2011-06-01	2017-04-11	Spiber Inc.	Artificial polypeptide fiber and method for producing the same
EP2868782B1 (fr) *	2012-06-28	2020-07-15	Spiber Inc.	Fibre de protéine teintée dans la masse et procédé pour produire celle-ci
EP3046585B1 (fr)	2013-09-17	2021-08-25	Bolt Threads, Inc.	Procédés et compositions pour synthétiser des fibres de soie améliorées
US9907815B2 (en) *	2013-11-21	2018-03-06	The University Of Akron	Method for preparation of filaments of poly(α-lipoic acid) polymers
KR102402443B1 (ko)	2015-03-16	2022-05-30	볼트 쓰레즈, 인크.	개선된 실크 섬유
EP3281948B1 (fr)	2015-04-09	2020-06-10	Spiber Inc.	Solution de solvant polaire et procédé de production associé
WO2016163337A1 (fr)	2015-04-09	2016-10-13	Ｓｐｉｂｅｒ株式会社	Solution de solvant polaire et procédé de production associé
EP3307765B1 (fr)	2015-06-11	2024-04-10	Bolt Threads, Inc.	Fils de fibres de protéine recombinée ayant des propriétés améliorées
AU2016294611B2 (en)	2015-07-14	2022-08-11	Evolved By Nature, Inc.	Silk performance apparel and products and methods of preparing the same
US10981959B2 (en) *	2015-08-10	2021-04-20	Seevix Material Sciences Ltd.	Compositions and methods for fabricating synthetic dragline spider silk
JP2018159137A (ja)	2015-08-20	2018-10-11	国立研究開発法人理化学研究所	クモ糸様構造を有するポリペプチド繊維の製造方法
JP6848173B2 (ja) *	2015-10-09	2021-03-24	東レ株式会社	含繊維結晶、含繊維結晶の製造方法、含繊維結晶の製造装置および薬剤ソーキング装置
KR102790669B1 (ko) *	2016-02-11	2025-04-04	시비스 머테리얼 사이언스 리미티드	합성 드래그라인 거미 실크를 포함하는 복합체
RU2018135566A (ru) *	2016-04-28	2020-05-28	Спайбер Инк.	Модифицированный фиброин
EP3469121A4 (fr)	2016-06-10	2020-01-08	Bolt Threads, Inc.	Fils de fibres de protéine recombinante ayant des propriétés améliorées
EP3502169B1 (fr) *	2016-08-19	2021-08-25	Riken	Composition de moulage composite comprenant une protéine de type fibroïne, et procédé de production de la composition de moulage composite
EP3512871A4 (fr)	2016-09-14	2020-07-29	Bolt Threads, Inc.	Fibres de protéines recombinantes uniformes longues
DE102016222480B4 (de) *	2016-11-16	2020-02-13	Adidas Ag	Bekleidungsstück, das Spinnenseide aufweist oder Schuh, der Spinnenseide aufweist, und ein entsprechendes Herstellungsverfahren
JP6337252B1 (ja)	2017-03-10	2018-06-06	Ｓｐｉｂｅｒ株式会社	高収縮人造フィブロイン繊維及びその製造方法、並びに人造フィブロイン繊維の収縮方法
JP2020097796A (ja) *	2017-03-10	2020-06-25	Ｓｐｉｂｅｒ株式会社	人造フィブロイン繊維
US11692015B2 (en)	2017-07-26	2023-07-04	Spiber Inc.	Modified fibroin
JP2021080572A (ja) *	2018-01-31	2021-05-27	Ｓｐｉｂｅｒ株式会社	油剤付着タンパク質捲縮繊維の製造方法
US20210095399A1 (en) *	2018-04-03	2021-04-01	Spiber Inc.	Composite Fibers and Method for Manufacturing Same
WO2019194258A1 (fr) *	2018-04-03	2019-10-10	長谷虎紡績株式会社	Fil mélangé, corps tricoté/tissé de celui-ci et procédé de fabrication dudit corps tricoté/tissé
EP3833524A4 (fr)	2018-08-10	2022-06-22	Bolt Threads, Inc.	Composition pour un corps moulé
EP4139338A4 (fr)	2020-04-23	2025-07-09	Seevix Mat Sciences Ltd	Fibres de soie d'araignée modifiées et leur utilisation
CN116438228A (zh)	2020-08-14	2023-07-14	3D生物纤维公司	聚合物链和用于制备聚合物链的方法
CN113136635A (zh) *	2021-04-20	2021-07-20	徐建平	一种玉米肽纤维、制备方法及其应用
EP4252549A1 (fr)	2022-03-28	2023-10-04	Mirai Foods AG	Procédés et compositions de préparation de faisceaux musculaires fibreux pour la production de viande d'élevage

Citations (3)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
RU2201765C2 (ru) *	1995-10-25	2003-04-10	Транскариотик Терапиз, Инк.	Гибридные матричные имплантаты и эксплантаты
EP1462548A1 (fr) *	2002-01-04	2004-09-29	Guanqi Li	Fibre synthetique de phytoproteine et son procede de production
RU2008131298A (ru) *	2005-12-30	2010-02-10	Спибер Текнолоджиз Аб (Se)	Белки шелка паука и способы получения белков шелка паука

Family Cites Families (9)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
WO2003057727A1 (fr)	2002-01-11	2003-07-17	Nexia Biotechnologies, Inc.	Procedes de production de polypeptides de soie et de produits de ceux-ci
WO2003060099A2 (fr) *	2002-01-11	2003-07-24	Nexia Biotechnologies, Inc.	Procedes et appareils de filage d'une proteine de soie d'araignee
EP2662211A1 (fr) *	2002-06-24	2013-11-13	Tufts University	Biomatériaux à base de soie et leurs procédés d'utilisation
CN102532295B (zh)	2004-07-22	2014-10-15	Am丝绸有限责任公司	重组蜘蛛丝蛋白
CN100420777C (zh) *	2005-02-05	2008-09-24	李官奇	有吸波、屏蔽、吸热功能的蛋白质纤维纺丝原液及其制法
US20090123967A1 (en)	2005-08-29	2009-05-14	Thomas Scheibel	Modified spider silk proteins
CN100540760C (zh) *	2006-12-12	2009-09-16	新华锦集团有限公司	一种改性聚丙烯腈类纤维及其制造方法和用途
CN101855239B (zh)	2007-06-20	2013-11-06	巴斯夫欧洲公司	合成的重复蛋白及其生产和用途
WO2010057142A2 (fr) *	2008-11-17	2010-05-20	Trustees Of Tufts College	Modification de surface de matrices de fibroïne de soie avec du poly(éthylène glycol) utilisable comme barrière anti-adhérence et matériau anti-thrombose

2010
- 2010-03-17 WO PCT/EP2010/001694 patent/WO2011113446A1/fr not_active Ceased
2011
- 2011-03-16 WO PCT/EP2011/001307 patent/WO2011113592A1/fr not_active Ceased
- 2011-03-16 US US13/634,484 patent/US20130172478A1/en not_active Abandoned
- 2011-03-16 RU RU2012144053/05A patent/RU2545331C2/ru active
- 2011-03-16 AU AU2011229482A patent/AU2011229482B2/en not_active Ceased
- 2011-03-16 CA CA2789647A patent/CA2789647C/fr active Active

Patent Citations (3)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
RU2201765C2 (ru) *	1995-10-25	2003-04-10	Транскариотик Терапиз, Инк.	Гибридные матричные имплантаты и эксплантаты
EP1462548A1 (fr) *	2002-01-04	2004-09-29	Guanqi Li	Fibre synthetique de phytoproteine et son procede de production
RU2008131298A (ru) *	2005-12-30	2010-02-10	Спибер Текнолоджиз Аб (Se)	Белки шелка паука и способы получения белков шелка паука

Cited By (1)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
RU2769982C2 (ru) *	2016-04-28	2022-04-12	Спайбер Инк.	Модифицированный фиброин

Also Published As

Publication number	Publication date
RU2012144053A (ru)	2014-04-27
CA2789647A1 (fr)	2011-09-22
AU2011229482B2 (en)	2015-05-07
WO2011113592A1 (fr)	2011-09-22
WO2011113446A1 (fr)	2011-09-22
CA2789647C (fr)	2016-04-26
AU2011229482A1 (en)	2012-08-30
US20130172478A1 (en)	2013-07-04

Publication	Publication Date	Title
RU2545331C2 (ru)	2015-03-27	Способ получения полимерсодержащих волокон
Rammensee et al.	2006	Rheological characterization of hydrogels formed by recombinantly produced spider silk
Rising et al.	2022	Biological materials processing: time-tested tricks for sustainable fiber fabrication
US11248120B2 (en)	2022-02-15	Methods for producing high toughness silk fibres
Saravanan	2006	Spider silk-structure, properties and spinning
JP5128943B2 (ja)	2013-01-23	組換えスパイダーシルクタンパク質
Mandal et al.	2010	Biospinning by silkworms: silk fiber matrices for tissue engineering applications
Mandal et al.	2008	Non‐bioengineered silk gland fibroin protein: Characterization and evaluation of matrices for potential tissue engineering applications
Debabov et al.	2020	Recombinant spidroins as the basis for new materials
EP3334754B1 (fr)	2024-12-18	Compositions et procédés de fabrication de soie de fil de traîne d'araignée synthétique
US20080293918A1 (en)	2008-11-27	Method and apparatus for extraction of protein material from arthropod glands and a membrane formed therefrom
WO2015127711A1 (fr)	2015-09-03	Procédé de préparation et utilisation d'hydrogel de séricine
JP2008507260A (ja)	2008-03-13	天然起源のタンパク質およびそれから作られる材料
Zhou et al.	2020	Evaluation of the potential of chimeric spidroins/poly (L-lactic-co-ε-caprolactone)(PLCL) nanofibrous scaffolds for tissue engineering
US12570722B2 (en)	2026-03-10	Single alpha chain collagens
Hsia et al.	2011	Spider silk composites and applications
CN111094326A (zh)	2020-05-01	用于产生丝融合蛋白的浓缩粘合相的方法
EP2547810B1 (fr)	2019-03-06	Procédé de fabrication de fibres contenant un polymère
Yazawa et al.	2023	Wild silkworm cocoon waste conversion into tough regenerated silk fibers by solution spinning
Zhang et al.	2021	Characteristics of electrospun membranes in different spidroin/PCL ratios
WO2003069033A1 (fr)	2003-08-21	Materiaux a base de proteine helicoidale - $g(a) et procedes de fabrication de ces derniers
Breslauer et al.	2012	9.04-Silks
Kandhavadivu et al.	2023	A Study on the application of Weaver ant silk in wound healing
Heidebrecht	2018	Production and characterization of artificial spider silk fibers with the same toughness as natural dragline silk fibers
CN117966297B (zh)	2024-09-24	一种利用微流控纺丝技术制备植物蛋白纤维的方法

RU2545331C2 - Способ получения полимерсодержащих волокон - Google Patents

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Landscapes

Applications Claiming Priority (3)

Publications (2)

Family

ID=43035008

Family Applications (1)

Country Status (5)

Cited By (1)

Families Citing this family (29)

Citations (3)

Family Cites Families (9)

Patent Citations (3)

Cited By (1)

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