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<p>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 <i>cross-β-strand linking</i>, 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 &lt;15% of the total β-strands in the amyloidogenic aggregates, but they can mediate a significant proportion of intermolecular interactions, operating as dynamic molecular adapters that regulate the inter-β-sheet packing geometry. Crucially, these linkers exist as conformational ensembles of heterogeneous substates, bestowing remarkable structural diversity to the aggregates. Through promiscuous engagement with multiple conformational substates, cross-β-strand linkers enable the aggregates to balance order and disorder. In this work, we provide a perspective on how low-abundance structural elements can orchestrate complex molecular architectures in assembly systems.</p>

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

  • 期刊论文

  • 出版模式：

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  • 发表日期：

    2026年1月6日

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  • Shanshan Mo,
  • Ruonan Wang,
  • Zhongyi Jian,
  • Mingwei Liu,
  • Feiyi Zhang,
  • Zhun Deng,
  • Wenbo Zhang,
  • Yanlian Yang,
  • Chen Wang,
  • Lanlan Yu,
  • Mingzhan Wang,
  • Chenxuan Wang

摘要

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 <15% of the total β-strands in the amyloidogenic aggregates, but they can mediate a significant proportion of intermolecular interactions, operating as dynamic molecular adapters that regulate the inter-β-sheet packing geometry. Crucially, these linkers exist as conformational ensembles of heterogeneous substates, bestowing remarkable structural diversity to the aggregates. Through promiscuous engagement with multiple conformational substates, cross-β-strand linkers enable the aggregates to balance order and disorder. In this work, we provide a perspective on how low-abundance structural elements can orchestrate complex molecular architectures in assembly systems.