Structural highlights
Publication Abstract from PubMedThe self-assembly of peptides into amyloid fibrils enables the design of functional biomaterials, yet the conformational constraints of alpha-peptides limit the attainable supramolecular diversity. Here, we introduce beta-amino acids, beta-phenylalanine (beta-Phe), and beta-homophenylalanine (beta-hPhe) into the reversible fibril-forming core sequence hnRAC1 to generate alpha/beta-peptide variants with distinct architectures and enhanced thermal stability. Cryo-EM reveals that beta-modified peptides assemble into polymorphic fibrils with cross-beta structures that differ markedly from each other and from native hnRAC1. Comparative structural analysis indicates that backbone extension by beta-residues increases subunit conformational heterogeneity, enabling tighter packing and formation of more thermostable fibrils. Examination of intra- and intermolecular contacts shows that enhanced pi-pi stacking, hydrophobic interactions, hydrogen bonds, and electrostatic interactions likely contribute to fibril stabilization. These results show that minimal backbone modifications can remodel amyloid architecture, offering a generalizable strategy for designing structurally diverse and robust peptide-based biomaterials. Conformational Adaptability and Thermostability in alpha/beta-Peptide Fibrils Induced by beta-Amino Acid Substitution.,Li Y, Li D, Yao Y, Liu K, Zhao Q, Zhang Y, Xu Y, Li D, Sun B, Liu C, Dai B Nano Lett. 2025 Dec 20. doi: 10.1021/acs.nanolett.5c05223. PMID:41420871[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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