Tyrosine residues mediate supercontraction in biomimetic spider silk

Gabriele Greco; Tina Arndt; Benjamin Schmuck; Juanita Francis; Fredrik G. Bäcklund; Olga Shilkova; Andreas Barth; Nathalie Gonska; Gulaim Seisenbaeva; Vadim Kessler; Jan Johansson; Nicola M. Pugno; Anna Rising

doi:10.1038/s43246-021-00147-w

Communications Materials (Apr 2021)

Tyrosine residues mediate supercontraction in biomimetic spider silk

Gabriele Greco,
Tina Arndt,
Benjamin Schmuck,
Juanita Francis,
Fredrik G. Bäcklund,
Olga Shilkova,
Andreas Barth,
Nathalie Gonska,
Gulaim Seisenbaeva,
Vadim Kessler,
Jan Johansson,
Nicola M. Pugno,
Anna Rising

Affiliations

Gabriele Greco: Laboratory of Bio-Inspired, Bionic, Nano, Meta, Materials & Mechanics, Department of Civil, Environmental and Mechanical Engineering, University of Trento
Tina Arndt: Department of Biosciences and Nutrition, Karolinska Institutet
Benjamin Schmuck: Department of Biosciences and Nutrition, Karolinska Institutet
Juanita Francis: Department of Biosciences and Nutrition, Karolinska Institutet
Fredrik G. Bäcklund: Department of Biosciences and Nutrition, Karolinska Institutet
Olga Shilkova: Department of Biosciences and Nutrition, Karolinska Institutet
Andreas Barth: Department of Biochemistry and Biophysics, Svante Arrhenius väg 16C, Stockholm University
Nathalie Gonska: Department of Anatomy, Physiology and Biochemistry, Swedish University of Agricultural Sciences
Gulaim Seisenbaeva: Department of Molecular Sciences, Swedish University of Agricultural Sciences
Vadim Kessler: Department of Molecular Sciences, Swedish University of Agricultural Sciences
Jan Johansson: Department of Biosciences and Nutrition, Karolinska Institutet
Nicola M. Pugno: Laboratory of Bio-Inspired, Bionic, Nano, Meta, Materials & Mechanics, Department of Civil, Environmental and Mechanical Engineering, University of Trento
Anna Rising: Department of Biosciences and Nutrition, Karolinska Institutet

DOI: https://doi.org/10.1038/s43246-021-00147-w
Journal volume & issue: Vol. 2, no. 1
pp. 1 – 10

Abstract

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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.

Published in Communications Materials

ISSN: 2662-4443 (Online)
Publisher: Nature Portfolio
Country of publisher: United States
LCC subjects: Technology: Electrical engineering. Electronics. Nuclear engineering: Materials of engineering and construction. Mechanics of materials
Website: https://www.nature.com/commsmat/

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