初始二级结构对蜘蛛丝蛋白凝胶构象和机械性能的影响

IF 5.4 2区医学 Q2 MATERIALS SCIENCE, BIOMATERIALS

ACS Biomaterials Science & Engineering Pub Date : 2024-09-17 DOI:10.1021/acsbiomaterials.4c00809

Takanori Higashi, Hideyasu Okamura, Takehiro K. Sato, Takashi Morinaga, Ryo Satoh, Yu Suzuki

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引用次数: 0

摘要

重组蜘蛛丝蛋白（RSP）是一种很有前途的生物材料，可用于开发不依赖化石燃料的高性能材料。在这项研究中，我们探讨了 RSP 初始二级结构对基于 RSP 的水凝胶性能的影响。通过溶剂处理将 RSP 的初始结构改变为 β-片（β-RSP）、α-螺旋（α-RSP）和无规线圈（rc-RSP），我们比较了所得凝胶的结构和机械性能。固态核磁共振显示所有凝胶都具有富含β片层的结构，与rc-RSP凝胶相比，α-RSP凝胶的强度和杨氏模量明显更高。X 射线衍射显示，α-RSP 凝胶具有独特的晶体结构，有别于 β-RSP 和 rc-RSP 凝胶。不同的初始二级结构可能会导致凝胶中分子链的结晶和网络结构发生变化，从而解释了为什么在 α-RSP 凝胶中观察到了优异的机械性能。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

Influence of Initial Secondary Structure on Conformation and Mechanical Properties of Spider Silk Protein Gels

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Influence of Initial Secondary Structure on Conformation and Mechanical Properties of Spider Silk Protein Gels

Recombinant spider silk protein (RSP) is a promising biomaterial for developing high-performance materials independent of fossil fuels. In this study, we investigated the influence of the initial secondary structure of RSPs on the properties of RSP-based hydrogels. By altering the initial structure of RSP to β-sheets (β-RSP), α-helices (α-RSP), and random coils (rc-RSP) through solvent treatment, we compared the structures and mechanical properties of the resulting gels. Solid-state NMR revealed a β-sheet-rich structure in all gels, with the α-RSP gel exhibiting significantly higher strength and Young’s modulus compared to the rc-RSP gel. X-ray diffraction revealed that the α-RSP gel had a unique crystalline structure, distinguishing it from the β-RSP and rc-RSP gels. The different initial secondary structures possibly lead to variations in the crystalline and network structures of the molecular chains within the gels, explaining the superior mechanical properties observed in the α-RSP gels.

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来源期刊

ACS Biomaterials Science & Engineering Materials Science-Biomaterials

CiteScore

10.30

自引率

3.40%

发文量

413

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