AI Article Synopsis
- Recombinant spider silk protein (RSP) shows potential as a sustainable biomaterial for creating high-performance materials.
- This study explored how the initial secondary structure of RSP (β-sheets, α-helices, and random coils) impacts the mechanical properties of resulting hydrogels.
- Findings indicated that gels made from α-RSP had significantly better strength and stiffness than those made from random coils, due to unique crystalline structures formed during solvent treatment.
Article 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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| http://dx.doi.org/10.1021/acsbiomaterials.4c00809 | DOI Listing |
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