Atypical β-strand insertion mediates the noncovalent cross-linking in amyloid aggregates

Nature Communications 2026 Open access

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Authors: Shimin Mo, Ruonan Wang, Zhongyi Jian, Ming Liu, F K Zhang, Zhun Deng, Wen Zhang, YanLian YANG, Chen Wang, Chen Wang, Lanlan Yu, Mingzhan Wang
+2 more Chenxuan Wang, Chenxuan Wang
DOI: 10.1038/s41467-025-68185-3
Cited by: 1
References: 51

Abstract

β-Strand motifs are essential recognition modules in protein-protein interactions (PPIs), which govern cellular signaling networks and regulate molecular pathway dynamics. Herein we present an unexpected discovery of a previously uncharacterized β-strand insertion mechanism termed as cross-β-strand linking, wherein β-strands within the β-sheet-rich aggregates form inter-β-sheet connections through insertion into adjacent β-sheets. These cross-β-strand linkers comprise

Fields of Study & Subjects

Alzheimer's disease research and treatments Supramolecular Self-Assembly in Materials Protein Structure and Dynamics

Publication details

Journal / source
Nature Communications
Publisher
Springer Science and Business Media LLC
Volume
17
Issue
1
Pages
1449–1449
Publication date
6 January 2026
Language
EN