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<p>Silk-spinning organisms naturally produce fibers with extraordinary properties at minimal energy input. Silk protein (fibroin) feedstock’s instability limits the mechanistic exploration of silk fiber formation to in-vitro studies of certain gland sections, offering a fragmented, non-native view of this process. Here, we unveil key events of fibroin stage-wise macromolecular assembly and structural transitions, essential for liquid feedstock storage and conversion into hierarchically structured solid fibers. By combining cryo-electron microscopy techniques, we monitor silk feedstock processing in-situ, at the nano-to-micron scales, along <i>Bombyx mori</i> silk gland and reveal nano-scale organizations. During storage, fibroin forms micron-sized spherical “compartments”, ensuring protein stability and avoiding premature fibrillation. The spinning itself starts after the compartments’ disassembly. It commences via a series of structural transitions, from protein alignment to forming several fibrillated nano-structures and, finally, a network of physically cross-linked nano-bundles, determining the final silk fiber structure and properties.</p>

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The stage-wise macromolecular assembly and structure evolution of silk along the silk gland

  • 期刊论文

  • 出版模式：

    开放获取

  • 发表日期：

    2026年6月1日

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  • Ori Brookstein,
  • Eyal Shimoni,
  • Dror Eliaz,
  • Nili Dezorella,
  • Ehud Sivan,
  • Idan Biran,
  • Israel Greenfeld,
  • Katya Rechav,
  • Anna Kozell,
  • H. Daniel Wagner,
  • Ulyana Shimanovich

摘要

Silk-spinning organisms naturally produce fibers with extraordinary properties at minimal energy input. Silk protein (fibroin) feedstock’s instability limits the mechanistic exploration of silk fiber formation to in-vitro studies of certain gland sections, offering a fragmented, non-native view of this process. Here, we unveil key events of fibroin stage-wise macromolecular assembly and structural transitions, essential for liquid feedstock storage and conversion into hierarchically structured solid fibers. By combining cryo-electron microscopy techniques, we monitor silk feedstock processing in-situ, at the nano-to-micron scales, along Bombyx mori silk gland and reveal nano-scale organizations. During storage, fibroin forms micron-sized spherical “compartments”, ensuring protein stability and avoiding premature fibrillation. The spinning itself starts after the compartments’ disassembly. It commences via a series of structural transitions, from protein alignment to forming several fibrillated nano-structures and, finally, a network of physically cross-linked nano-bundles, determining the final silk fiber structure and properties.