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Tyrosine residues mediate supercontraction in biomimetic spider silk

Greco, Gabriele and Arndt, Tina and Schmuck, Benjamin and Francis, Juanita and Bäcklund, Fredrik G. and Shilkova, Olga and Barth, Andreas and Gonska, Nathalie and Seisenbaeva, Gulaim and Kessler, Vadim and Johansson, Jan and Pugno, Nicola M. and Rising, Anna (2021). Tyrosine residues mediate supercontraction in biomimetic spider silk. Communications Materials. 2 , 43
[Research article]

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Abstract

Water and humidity severely affect the material properties of spider major ampullate silk, causing the fiber to become plasticized, contract, swell and undergo torsion. Several amino acid residue types have been proposed to be involved in this process, but the complex composition of the native fiber complicates detailed investigations. Here, we observe supercontraction in biomimetically produced artificial spider silk fibers composed of defined proteins. We found experimental evidence that proline is not the sole residue responsible for supercontraction and that tyrosine residues in the amorphous regions of the silk fiber play an important role. Furthermore, we show that the response of artificial silk fibers to humidity can be tuned, which is important for the development of materials for applications in wet environments, eg producing water resistant fibers with maximal strain at break and toughness modulus.

Authors/Creators:Greco, Gabriele and Arndt, Tina and Schmuck, Benjamin and Francis, Juanita and Bäcklund, Fredrik G. and Shilkova, Olga and Barth, Andreas and Gonska, Nathalie and Seisenbaeva, Gulaim and Kessler, Vadim and Johansson, Jan and Pugno, Nicola M. and Rising, Anna
Title:Tyrosine residues mediate supercontraction in biomimetic spider silk
Series Name/Journal:Communications Materials
Year of publishing :2021
Volume:2
Article number:43
Number of Pages:10
ISSN:2662-4443
Language:English
Publication Type:Research article
Article category:Scientific peer reviewed
Version:Published version
Copyright:Creative Commons: Attribution 4.0
Full Text Status:Public
Subjects:(A) Swedish standard research categories 2011 > 1 Natural sciences > 104 Chemical Sciences > Materials Chemistry
(A) Swedish standard research categories 2011 > 2 Engineering and Technology > 209 Industrial Biotechnology > Bio Materials
(A) Swedish standard research categories 2011 > 3 Medical and Health Sciences > 304 Medical Biotechnology > Biomaterials Science
URN:NBN:urn:nbn:se:slu:epsilon-p-114644
Permanent URL:
http://urn.kb.se/resolve?urn=urn:nbn:se:slu:epsilon-p-114644
Additional ID:
Type of IDID
DOI10.1038/s43246-021-00147-w
ID Code:26367
Faculty:VH - Faculty of Veterinary Medicine and Animal Science
NJ - Fakulteten för naturresurser och jordbruksvetenskap
Department:(VH) > Dept. of Anatomy, Physiology and Biochemistry
(NL, NJ) > Department of Molecular Sciences
Deposited By: SLUpub Connector
Deposited On:21 Dec 2021 15:25
Metadata Last Modified:21 Dec 2021 15:31

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