Intermediate States Enable Keratin-like α-To-β Transformations in Strain-Responsive Synthetic Polypeptides DOI
Tianjian Yang,

Jianan Mao,

Tianrui Xue

et al.

Journal of the American Chemical Society, Journal Year: 2025, Volume and Issue: unknown

Published: April 22, 2025

Nature's fibrous proteins, such as α-keratin, achieve remarkable mechanical properties by undergoing strain-induced α-to-β conformational transitions. Inspired these materials, we report a strategy for designing synthetic polypeptides that undergo similar transformations at elevated temperatures far exceeding keratin's operational range. By employing helix-confined ring-opening polymerization (ROP) of N-carboxyanhydrides (NCAs) initiated short poly(γ-benzyl-l-glutamate) (PBLG) precursor, synthesized poly(O-benzyl-l-serine) (PBLS) chains adopt an α-helical structure yet transition into β-sheets upon heating. Compression molding carefully chosen drives PBLS segments α-β intermediate state, characterized relaxed intrachain hydrogen bonds and hexagonal packing arrangement. Under strain, states convert in situ β-sheets, producing significant strain-hardening well below the spontaneous temperature threshold. This approach extends to bearing different side chains, poly(S-benzyl-l-cysteine), demonstrating robust reinforcement across wide window up ∼ 200 °C. In synchrotron X-ray analysis confirms chain alignment, β-sheet formation, domain growth occur stepwise during deformation. harnessing supramolecular cooperativity conferred compression-molded films, our method provides versatile platform developing next-generation polypeptide materials with tunable resilience responsiveness─surpassing limitations natural proteins enabling potential applications demanding broad-temperature adaptability.

Language: Английский

Ion transport in helical-helical polypeptide polymerized ionic liquid block copolymers DOI Creative Commons

Yingying Chen,

Tianjian Yang, Yao Lin

et al.

Nature Communications, Journal Year: 2025, Volume and Issue: 16(1)

Published: March 12, 2025

Helical-helical polypeptide polymerized ionic liquid block copolymers (PPIL BCPs) are synthesized to investigate the role of helical structure on self-assembly and conductivity. PPIL BCPs, consisting a cationic (PTPLG) with bis(trifluoromethane sulfonimide) (TFSI) counterion varying lengths connected length-fixed neutral poly-(γ-benzyl-L-glutamate) (PBLG) block, exhibit stable conformations minimal glass transition (Tg) variation. Here, we show that increasing PIL composition leads from poorly ordered highly lamellar (LAM) structures highest content BCP forming bilayer LAM close-packed helices. This morphology yields 1.5 order magnitude higher Tg- volume fraction-normalized conductivity factor f > 0.8 compared less BCPs < 0.05 = 2/3 for ideal lamellae. These results highlight critical in optimizing ion transport, offering design strategy high-performance solid electrolytes. Ion transport polymers is important applications energy devices, but many have not been widely considered. authors report use importance secondary

Language: Английский

Citations

0
Intermediate States Enable Keratin-like α-To-β Transformations in Strain-Responsive Synthetic Polypeptides DOI
Tianjian Yang,

Jianan Mao,

Tianrui Xue

et al.

Journal of the American Chemical Society, Journal Year: 2025, Volume and Issue: unknown

Published: April 22, 2025

Nature's fibrous proteins, such as α-keratin, achieve remarkable mechanical properties by undergoing strain-induced α-to-β conformational transitions. Inspired these materials, we report a strategy for designing synthetic polypeptides that undergo similar transformations at elevated temperatures far exceeding keratin's operational range. By employing helix-confined ring-opening polymerization (ROP) of N-carboxyanhydrides (NCAs) initiated short poly(γ-benzyl-l-glutamate) (PBLG) precursor, synthesized poly(O-benzyl-l-serine) (PBLS) chains adopt an α-helical structure yet transition into β-sheets upon heating. Compression molding carefully chosen drives PBLS segments α-β intermediate state, characterized relaxed intrachain hydrogen bonds and hexagonal packing arrangement. Under strain, states convert in situ β-sheets, producing significant strain-hardening well below the spontaneous temperature threshold. This approach extends to bearing different side chains, poly(S-benzyl-l-cysteine), demonstrating robust reinforcement across wide window up ∼ 200 °C. In synchrotron X-ray analysis confirms chain alignment, β-sheet formation, domain growth occur stepwise during deformation. harnessing supramolecular cooperativity conferred compression-molded films, our method provides versatile platform developing next-generation polypeptide materials with tunable resilience responsiveness─surpassing limitations natural proteins enabling potential applications demanding broad-temperature adaptability.

Language: Английский

Citations

0