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

被引：29

作者：

Otikovs, Martins ^{[1
]}

Andersson, Marlene ^{[2
]}

Jia, Qiupin ^{[3
]}

Nordling, Kerstin ^{[4
]}

Meng, Qing ^{[3
]}

Andreas, Loren B. ^{[5
]}

Pintacuda, Guido ^{[5
]}

Johansson, Jan ^{[4
]}

Rising, Anna ^{[2
,4
]}

Jaudzems, Kristaps ^{[1
]}

机构：

[1] Latvian Inst Organ Synth, Aizkraukles 21, LV-1006 Riga, Latvia

[2] Swedish Univ Agr Sci, Dept Anat Physiol & Biochem, Box 7011, S-75007 Uppsala, Sweden

[3] Donghua Univ, Inst Biol Sci & Biotechnol, Shanghai 201620, Peoples R China

[4] Karolinska Inst, Ctr Alzheimer Res, Dept Neurobiol Care Sci & Soc NVS, S-14157 Huddinge, Sweden

[5] Univ Lyon, Ctr RMN Tres Hauts Champs, UMR CNRS 5280, Inst Sci Analyt,UCB Lyon 1,ENS Lyon, 5 Rue Doua, F-69100 Villeurbanne, France

来源：

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION | 2017年 / 56卷 / 41期

基金：

瑞典研究理事会;

关键词：

biomimicry; fibrous proteins; NMR spectroscopy; spider silk; PH-DEPENDENT DIMERIZATION; MECHANICAL-PROPERTIES; SECONDARY STRUCTURE; TERMINAL DOMAIN; PROTEINS; FIBERS; SWITCH;

D O I：

10.1002/anie.201706649

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

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.

引用

页码：12571 / 12575

页数：5

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