Degree of Biomimicry of Artificial Spider Silk Spinning Assessed by NMR Spectroscopy

Abstract

Biomimetic spinning of artificial spider silk requires that the terminal domains of designed minispidroins undergo specific structural changes in concert with the beta-sheet conversion of the repetitive region. Herein, we combine solution and solid-state NMR methods to probe domain-specific structural changes in the NT2RepCT minispidroin, which allows us to assess the degree of biomimicry of artificial silk spinning. In addition, we show that the structural effects of post-spinning procedures can be examined. By studying the impact of NT2RepCT fiber drying, we observed a reversible beta-to-alpha conversion. We think that this approach will be useful for guiding the optimization of artificial spider silk fibers.

Keywords

biomimicry; fibrous proteins; NMR spectroscopy; spider silk

Published in

Angewandte Chemie International Edition
2017, volume: 56, number: 41, pages: 12571-12575
Publisher: WILEY-V C H VERLAG GMBH

SLU Authors

• Andersson, Marlene

  • Department of Animal Biosciences, Swedish University of Agricultural Sciences
    

• Nordling, Kerstin

  • Karolinska Institute

• Johansson, Jan

  • Karolinska Institute

• Rising, Anna

  • Department of Animal Biosciences, Swedish University of Agricultural Sciences
    

UKÄ Subject classification

Molecular Biology
Biochemistry

Publication identifier

• DOI: https://doi.org/10.1002/anie.201706649

Permanent link to this page (URI)

https://res.slu.se/id/publ/90937