Structural highlights
Function
GLYG4_SOYBN Glycinin is the major seed storage protein of soybean (PubMed:2485233). Glycinin basic peptides (GBPs), and, to a lower extent, glycinin exhibit antibacterial activity against Gram-negative and Gram-positive bacteria (e.g. L.monocytogenes, B.subtilis, E.coli and S.enteritidis) by forming pores and aggregating in transmembranes, leading to membrane permeability and, eventually, cell death (PubMed:22236762, PubMed:28590128, Ref.17).[1] [2] [3] [4]
Publication Abstract from PubMed
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 A) 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 pi-stacking. These atomic structures establish fundamental structure-property relationships that will inform the rational design of plant protein-based nanomaterials.
Dual Hydrophilic-Hydrophobic Core Architecture in Soy Glycinin Amyloid Fibrils Revealed by Cryo-EM.,Li S, Li S, Cheng Y, Fang Y, Cao Q, Cao Y Adv Sci (Weinh). 2025 Aug 29:e09821. doi: 10.1002/advs.202509821. PMID:40883254[5]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Sitohy MZ, Mahgoub SA, Osman AO. In vitro and in situ antimicrobial action and mechanism of glycinin and its basic subunit. Int J Food Microbiol. 2012 Mar 1;154(1-2):19-29. PMID:22236762 doi:10.1016/j.ijfoodmicro.2011.12.004
- ↑ Nielsen NC, Dickinson CD, Cho TJ, Thanh VH, Scallon BJ, Fischer RL, Sims TL, Drews GN, Goldberg RB. Characterization of the glycinin gene family in soybean. Plant Cell. 1989 Mar;1(3):313-28. PMID:2485233 doi:10.1105/tpc.1.3.313
- ↑ Zhao GP, Li YQ, Sun GJ, Mo HZ. Antibacterial Actions of Glycinin Basic Peptide against Escherichia coli. J Agric Food Chem. 2017 Jun 28;65(25):5173-5180. PMID:28590128 doi:10.1021/acs.jafc.7b02295
- ↑ Li YQ, Hao M, Yang J, Mo HZ. Effects of glycinin basic polypeptide on sensory and physicochemical properties of chilled pork. Food Sci Biotechnol. 2016 Jun 30;25(3):803-809. PMID:30263339 doi:10.1007/s10068-016-0135-2
- ↑ Li S, Li S, Cheng Y, Fang Y, Cao Q, Cao Y. Dual Hydrophilic-Hydrophobic Core Architecture in Soy Glycinin Amyloid Fibrils Revealed by Cryo-EM. Adv Sci (Weinh). 2025 Aug 29:e09821. PMID:40883254 doi:10.1002/advs.202509821
