Authors
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
Published in
Nature communications. Volume 17. Issue 1. Mar 26, 2026. Epub Mar 26, 2026.
Abstract
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.
PMID:
41881998
Bibliographic data and abstract were imported from PubMed on 14 Jun 2026.
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