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

Martins Otikovs; Marlene Andersson; Qiupin Jia; Kerstin Nordling; Qing Meng; Loren B. Andreas; Guido Pintacuda; Jan Johansson; Anna Rising; Kristaps Jaudzems

doi:10.1002/anie.201706649

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

Martins Otikovs
, Marlene Andersson
, Qiupin Jia
, Kerstin Nordling
, Qing Meng
, Loren B. Andreas
, Guido Pintacuda
, Jan Johansson
, Anna Rising
, Kristaps Jaudzems^*

^*Corresponding author for this work

Latvian Institute of Organic Synthesis
Swedish University of Agricultural Sciences
Donghua University
Karolinska Institutet
École normale supérieure de Lyon

Research output: Contribution to journal › Article › peer-review

29 Citations (Scopus)

Abstract

Biomimetic spinning of artificial spider silk requires that the terminal domains of designed minispidroins undergo specific structural changes in concert with the β-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.

Original language	English
Pages (from-to)	12571-12575
Number of pages	5
Journal	Angewandte Chemie - International Edition
Volume	56
Issue number	41
DOIs	https://doi.org/10.1002/anie.201706649
Publication status	Published - 2 Oct 2017
Externally published	Yes

Keywords

NMR spectroscopy
biomimicry
fibrous proteins
spider silk

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10.1002/anie.201706649

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title = "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 β-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 = "NMR spectroscopy, biomimicry, fibrous proteins, spider silk",

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doi = "10.1002/anie.201706649",

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T1 - Degree of Biomimicry of Artificial Spider Silk Spinning Assessed by NMR Spectroscopy

AU - Otikovs, Martins

AU - Andersson, Marlene

AU - Jia, Qiupin

AU - Nordling, Kerstin

AU - Meng, Qing

AU - Andreas, Loren B.

AU - Pintacuda, Guido

AU - Johansson, Jan

AU - Rising, Anna

AU - Jaudzems, Kristaps

PY - 2017/10/2

Y1 - 2017/10/2

N2 - Biomimetic spinning of artificial spider silk requires that the terminal domains of designed minispidroins undergo specific structural changes in concert with the β-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.

AB - Biomimetic spinning of artificial spider silk requires that the terminal domains of designed minispidroins undergo specific structural changes in concert with the β-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.

KW - NMR spectroscopy

KW - biomimicry

KW - fibrous proteins

KW - spider silk

UR - https://www.scopus.com/pages/publications/85028708610

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DO - 10.1002/anie.201706649

M3 - Article

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AN - SCOPUS:85028708610

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JO - Angewandte Chemie - International Edition

JF - Angewandte Chemie - International Edition

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ER -

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

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Keywords

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