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TitleDual Hydrophilic-Hydrophobic Core Architecture in Soy Glycinin Amyloid Fibrils Revealed by Cryo-EM.
Journal, issue, pagesAdv Sci (Weinh), Vol. 12, Issue 41, Page e09821, Year 2025
Publish dateAug 29, 2025
AuthorsSaiya Li / Shuangjian Li / Yijia Cheng / Yapeng Fang / Qin Cao / Yiping Cao /
PubMed AbstractPlant-derived amyloid fibrils represent a promising class of sustainable nanomaterials outperforming their native counterparts in functionalities; however, the atomic-level structural mechanisms ...Plant-derived amyloid fibrils represent a promising class of sustainable nanomaterials outperforming their native counterparts in functionalities; however, the atomic-level structural mechanisms behind these enhancements have yet to be elucidated. Using cryo-EM, near-atomic resolution structures (3.4 and 3.5 Å) are determined for two distinct fibril polymorphs assembled in vitro from soy glycinin-A subunit. The dominant Type I fibril exhibits an unprecedented dual-core architecture, characterized by spatially segregated hydrophilic (Asp172-Asn178/Asn178'-Asp172') and hydrophobic (Val166-Ile168/Val186'-Pro184') domains, which contribute to a unique amyloid fold distinct from many known amyloid structures, including pathological and functional amyloids. In contrast, the minor Type II fibril adopts a conventional extended hydrophobic core with Tyr155-Tyr158 π-stacking. These atomic structures establish fundamental structure-property relationships that will inform the rational design of plant protein-based nanomaterials.
External linksAdv Sci (Weinh) / PubMed:40883254 / PubMed Central
MethodsEM (helical sym.)
Resolution3.41 - 3.52 Å
Structure data

64767

9v45

EMDB-64767, PDB-9v45:
Soy storage protein fibril (glycinin A) PM1
Method: EM (helical sym.) / Resolution: 3.41 Å

64778

9v4f

EMDB-64778, PDB-9v4f:
Soy storage protein fibril (glycinin A) PM2
Method: EM (helical sym.) / Resolution: 3.52 Å

Source
  • glycine max (soybean)
KeywordsPROTEIN FIBRIL / dual hydrophilic-hydrophobic / Soy storage protein fibril

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