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Updated: Jun 12, 2025

Material Formation of Recombinant Spider Silks through Aqueous Solvation using Heat and Pressure
Published on: May 6, 2019
Influence of Initial Secondary Structure on Conformation and Mechanical Properties of Spider Silk Protein Gels
Takanori Higashi1, Hideyasu Okamura1, Takehiro K Sato2
1Department of Applied Chemistry and Biotechnology, Graduate School of Engineering, University of Fukui, 3-9-1, Bunkyo, Fukui-shi, Fukui 910-8507, Japan.
Abstract:
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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