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

Angewandte Chemie International Edition 2017
Mārtiņš Otikovs, M. Andersson, Q. Jia, K. Nordling, Q. Meng, L.B. Andreas, G. Pintacuda, J. Johansson, A. Rising, Kristaps Jaudzems

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.

Atslēgas vārdi
Artificial Spider Silk Spinning, NMR Spectroscopy
DOI
10.1002/anie.201706649

Otikovs, M., Andersson, M., Jia, Q., Nordling, K., Meng, Q., Andreas, L., Pintacuda, G., Johansson, J., Rising, A., Jaudzems, K. Degree of Biomimicry of Artificial Spider Silk Spinning Assessed by NMR Spectroscopy.. Angewandte Chemie International Edition, 2017, Vol.56, Iss.41, 12571.-12575.lpp. ISSN 1433-7851. e-ISSN 1521-3773. Pieejams: doi:10.1002/anie.201706649

Publikācijas valoda
English (en)