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Tyrosine residues m...
Tyrosine residues mediate supercontraction in biomimetic spider silk
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Greco, Gabriele (author)
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Arndt, Tina (author)
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- Schmuck, Benjamin (author)
- Karolinska Institute
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Francis, Juanita (author)
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Bäcklund, Fredrik G. (author)
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Shilkova, Olga (author)
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- Barth, Andreas (author)
- Stockholms universitet,Institutionen för biokemi och biofysik
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- Gonska, Nathalie (author)
- Swedish University of Agricultural Sciences,Sveriges lantbruksuniversitet,Institutionen för anatomi, fysiologi och biokemi,Department of Anatomy, Physiology and Biochemistry (AFB)
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- Seisenbaeva, Gulaim (author)
- Swedish University of Agricultural Sciences,Sveriges lantbruksuniversitet,Institutionen för Molekylära vetenskaper,Department of Molecular Sciences
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- Kessler, Vadim (author)
- Swedish University of Agricultural Sciences,Sveriges lantbruksuniversitet,Institutionen för Molekylära vetenskaper,Department of Molecular Sciences
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Johansson, Jan (author)
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Pugno, Nicola M. (author)
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- Rising, Anna (author)
- Swedish University of Agricultural Sciences,Sveriges lantbruksuniversitet,Institutionen för anatomi, fysiologi och biokemi,Department of Anatomy, Physiology and Biochemistry (AFB),Karolinska Institute
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(creator_code:org_t)
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- 2021-04-12
- 2021
- English.
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In: Communications materials. - : Springer Science and Business Media LLC. - 2662-4443. ; 2:1
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Abstract
Subject headings
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- Exposing spider silk to wet conditions can cause supercontraction. Here, tyrosine amino acid residues within the amorphous regions are found to contribute to supercontraction, which can be controlled by protein engineering. 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.
Subject headings
- TEKNIK OCH TEKNOLOGIER -- Materialteknik (hsv//swe)
- ENGINEERING AND TECHNOLOGY -- Materials Engineering (hsv//eng)
- MEDICIN OCH HÄLSOVETENSKAP -- Medicinsk bioteknologi -- Biomaterialvetenskap (hsv//swe)
- MEDICAL AND HEALTH SCIENCES -- Medical Biotechnology -- Biomaterials Science (hsv//eng)
- NATURVETENSKAP -- Kemi -- Materialkemi (hsv//swe)
- NATURAL SCIENCES -- Chemical Sciences -- Materials Chemistry (hsv//eng)
- TEKNIK OCH TEKNOLOGIER -- Industriell bioteknik -- Biomaterial (hsv//swe)
- ENGINEERING AND TECHNOLOGY -- Industrial Biotechnology -- Bio Materials (hsv//eng)
Publication and Content Type
- ref (subject category)
- art (subject category)
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To the university's database
- By the author/editor
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Greco, Gabriele
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Arndt, Tina
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Schmuck, Benjami ...
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Francis, Juanita
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Bäcklund, Fredri ...
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Shilkova, Olga
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show more...
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Barth, Andreas
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Gonska, Nathalie
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Seisenbaeva, Gul ...
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Kessler, Vadim
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Johansson, Jan
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Pugno, Nicola M.
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Rising, Anna
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show less...
- About the subject
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- ENGINEERING AND TECHNOLOGY
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ENGINEERING AND ...
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and Materials Engine ...
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- MEDICAL AND HEALTH SCIENCES
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MEDICAL AND HEAL ...
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and Medical Biotechn ...
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and Biomaterials Sci ...
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- NATURAL SCIENCES
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NATURAL SCIENCES
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and Chemical Science ...
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and Materials Chemis ...
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- ENGINEERING AND TECHNOLOGY
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ENGINEERING AND ...
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and Industrial Biote ...
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and Bio Materials
- Articles in the publication
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Communications m ...
- By the university
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Stockholm University
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Swedish University of Agricultural Sciences