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July 30, 2026Nature CommunicationsOpen Access

Structural Basis of Amyloid Fibril Assembly by Plant Seed Storage Proteins

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Authors

YZYiling ZhangDLDanni LiQZQinyue Zhao

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Overview

Randomized trial reveals molecular basis of amyloid formation in plant seed proteins, highlighting potential food applications.

Key Points

  • This research aims to understand the structural basis of amyloid fibril formation by plant seed storage proteins.
  • Systematic assessment of oat 12S globulin, soybean 7S globulin, and rice glutelin under cooking-like conditions (pH 2, 85 °C).
  • Cryo-electron microscopy was used to determine the structure of oat globulin fibrils at 3.9 Å resolution.
  • Oat globulin and rice glutelin readily form fibrils in purified preparations and whole-seed extracts.
  • Soybean globulin forms fibrils only in purified preparations and remains largely amorphous in whole-seed extracts.
  • The oat globulin fibril core has a compact triangular architecture with pseudo-threefold symmetry, stabilized by extensive hydrophobic packing.

Cite This Study

Zhang et al. (2026) studied this question.

synapsesocial.com/papers/6a6af55560e2b924d3ea1736https://doi.org/10.1038/s41467-026-76001-9
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