<p>The intertwined strand arrangement in ropes, from micro- to macro-scale, results in tensile moduli significantly higher than those of single strands. Micro-scale ropes are found in biological systems, most commonly in mechanically-rigid collagen tri-strand arrangements. While human-made macro-ropes possess either left-handed (S) or right-handed (Z) twist, collagen exclusively adopts Z-twist architectures. Despite its natural abundance, the reconstruction and control of these supramolecular ropes in biomimetic systems using minimalist building units remains a fundamental challenge. Here, we demonstrate that cyclo-tryptophan-proline dipeptide stereoisomers self-assemble into complex crystalline supramolecular triple-helical structures. These unique architectures display tunable S- or Z-micro-rope-like twists governed by the configuration of tryptophan residues, as confirmed by co-assembly experiments and molecular dynamics simulations. Tensile testing revealed that these supramolecular micro-ropes exhibit significant moduli. These findings provide a potential platform for designing biomimetic functional helical materials with tunable supramolecular chirality and mechanical strength using minimalist building blocks.</p>

错误:搜索内容不能为空,请输入英文关键词
错误:关键词超出字数限制,请精简
高级检索

Formation of S- and Z-twist supramolecular micro-ropes by peptide stereoisomers

  • Hui Yuan,
  • Zhongyuan Yang,
  • Chengqian Yuan,
  • Sudha Shankar,
  • Aviad Levin,
  • Tiancheng Lv,
  • Zihan Wang,
  • Wei Sun,
  • Jadon Sitton,
  • Pierre-Andre Cazade,
  • Yoav Dan,
  • Yiming Tang,
  • Lihi Adler-Abramovich,
  • Yi Cao,
  • Sigal Rencus-Lazar,
  • Damien Thompson,
  • Dmitry Kurouski,
  • Tuomas P. J. Knowles,
  • Linda J. W. Shimon,
  • Guanghong Wei,
  • Bin Xue,
  • Rusen Yang,
  • Ehud Gazit

摘要

The intertwined strand arrangement in ropes, from micro- to macro-scale, results in tensile moduli significantly higher than those of single strands. Micro-scale ropes are found in biological systems, most commonly in mechanically-rigid collagen tri-strand arrangements. While human-made macro-ropes possess either left-handed (S) or right-handed (Z) twist, collagen exclusively adopts Z-twist architectures. Despite its natural abundance, the reconstruction and control of these supramolecular ropes in biomimetic systems using minimalist building units remains a fundamental challenge. Here, we demonstrate that cyclo-tryptophan-proline dipeptide stereoisomers self-assemble into complex crystalline supramolecular triple-helical structures. These unique architectures display tunable S- or Z-micro-rope-like twists governed by the configuration of tryptophan residues, as confirmed by co-assembly experiments and molecular dynamics simulations. Tensile testing revealed that these supramolecular micro-ropes exhibit significant moduli. These findings provide a potential platform for designing biomimetic functional helical materials with tunable supramolecular chirality and mechanical strength using minimalist building blocks.