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  Degree of biomimicry of artificial spider silk spinning assessed by NMR spectroscopy.

Otikovs, M., Andersson, M., Jia, Q., Nordling, K., Meng, Q., Andreas, L. B., et al. (2017). Degree of biomimicry of artificial spider silk spinning assessed by NMR spectroscopy. Angewandte Chemie International Edition, 56(41), 12571-12575. doi:10.1002/anie.201706649.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002E-2EC2-0 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002E-2EC6-8
Genre: Journal Article

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 Creators:
Otikovs, M., Author
Andersson, M., Author
Jia, Q., Author
Nordling, K., Author
Meng, Q., Author
Andreas, L. B.1, Author              
Pintacuda, G., Author
Johansson, J., Author
Rising, A., Author
Jaudzems, K., Author
Affiliations:
1Research Group of Solid State NMR Spectroscopy-2, MPI for Biophysical Chemistry, Max Planck Society, ou_2396693              

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 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.

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Language(s): eng - English
 Dates: 2017-08-302017-10-02
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1002/anie.201706649
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Title: Angewandte Chemie International Edition
Source Genre: Journal
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Pages: - Volume / Issue: 56 (41) Sequence Number: - Start / End Page: 12571 - 12575 Identifier: -