8ZM0

A self-assembled nanofiber

8ZM0 の概要

• エントリーDOI: 10.2210/pdb8zm0/pdb
• EMDBエントリー: 60234
• 分子名称: TYR-ALA-TRP-PHE (1 entity in total)
• 機能のキーワード: a chemically synthesized peptide that can be self-assembled into nanofiber, de novo protein
• 由来する生物種: synthetic construct
• タンパク質・核酸の鎖数: 62
• 化学式量合計: 36310.30

構造登録者

Shi, J.H.,Fang, Y.,Ma, D.,Wang, H.M. (登録日: 2024-05-21, 公開日: 2025-05-21, 最終更新日: 2025-12-24)

主引用文献

Fang, Y.,Shi, J.,Liang, J.,Ma, D.,Wang, H.
Water-regulated viscosity-plasticity phase transitions in a peptide self-assembled muscle-like hydrogel.
Nat Commun, 16:1058-1058, 2025

PubMed Abstract: The self-assembly of small molecules through non-covalent interactions is an emerging and promising strategy for building dynamic, stable, and large-scale structures. One remaining challenge is making the non-covalent interactions occur in the ideal positions to generate strength comparable to that of covalent bonds. This work shows that small molecule YAWF can self-assemble into a liquid-crystal hydrogel (LCH), the mechanical properties of which could be controlled by water. LCH can be used to construct stable solid threads with a length of over 1 meter by applying an external force on 2 µL of gel solution followed by water-regulated crystallization. These solid threads can support 250 times their weight. Cryogenic electron microscopy (Cryo-EM) analysis unravels the three-dimensional structure of the liquid-crystal fiber (elongated helix with C2 symmetry) at an atomic resolution. The multiscale mechanics of this material depend on the specificity of the molecular structure, and the water-controlled hierarchical and sophisticated self-assembly.

PubMed: 39865087
DOI: 10.1038/s41467-025-56415-7

実験手法

ELECTRON MICROSCOPY (3.1 Å)