Intermediate States Enable Keratin-like α‑To‑β Transformations in Strain-Responsive Synthetic Polypeptides

Nature’s fibrous proteins, such as α-keratin, achieve remarkable mechanical properties by undergoing strain-induced α-to-β conformational transitions. Inspired by these materials, we report a strategy for designing synthetic polypeptides that undergo similar transformations at elevated temperatures...

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Bibliographic Details
Main Author:	Tianjian Yang (11885819) (author)
Other Authors:	Jianan Mao (17734481) (author), Tianrui Xue (7615352) (author), Siyu Wu (286775) (author), Ruipeng Li (734290) (author), Yingying Chen (500738) (author), Abrar A. Sitab (21162420) (author), Jianjun Cheng (646595) (author), Yao Lin (1622536) (author)
Published:	2025
Subjects:	Biophysics Biochemistry Cell Biology Genetics Molecular Biology Biotechnology Evolutionary Biology Ecology Computational Biology Chemical Sciences not elsewhere classified Physical Sciences not elsewhere classified undergo similar transformations supramolecular cooperativity conferred responsiveness  surpassing ray analysis confirms hexagonal packing arrangement designing synthetic polypeptides wide temperature window tunable mechanical resilience ‑ β transformations β conformational transitions temperature mechanical adaptability β temperature threshold β intermediate state intermediate states convert situ synchrotron x sheets upon heating producing significant strain natural fibrous proteins like α ‑ generation polypeptide materials synthesized poly (< intermediate states fibrous proteins poly (< temperature limitations mechanical strain short poly versatile platform undergoing strain spontaneous α sheet formation operational range opening polymerization molded films method provides induced α hardening well employing helix developing next confined ring chain alignment approach extends >- carboxyanhydrides
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Intermediate States Enable Keratin-like α‑To‑β Transformations in Strain-Responsive Synthetic Polypeptides

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