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Publication Abstract from PubMed

The beta-lactoglobulin (beta-LG) protein, sourced from dietary products, is notable for forming amyloid fibrils, which are increasingly recognized as valuable protein-based nanomaterials due to their superior cytocompatibility, chemical resilience, and mechanical characteristics. However, the precise atomic details of beta-LG's fibril assembly are not understood. In this study, we utilized cryo-electron microscopy to elucidate the composition and architecture of beta-LG fibrils. We discovered that the beta-LG fibril was rapidly assembled after a short time incubation. Remarkably, these fibril cores were composed of the first 32 residues, forming four beta-strands that adopted a serpentine arrangement into a single protofilament. This protofilament core's stability was reinforced by hydrophobic interactions. Two identical protofilaments then align to form four distinct structural polymorphs through unique interfacial configurations, which were stabilized by hydrophilic interactions, hydrogen bonding, and electrostatic forces. Our findings provide a structural framework for understanding beta-LG fibril formation and pave the way for designing innovative beta-LG-based nanomaterials.

beta-Lactoglobulin Forms a Conserved Fibril Core That Assembles into Diverse Fibril Polymorphs.,Xu Y, Li D, Zhang Y, Zhao Q, Sun B, Liu C, Li D, Dai B Nano Lett. 2025 Mar 5;25(9):3653-3661. doi: 10.1021/acs.nanolett.5c00137. Epub , 2025 Feb 24. PMID:39992798^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.