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TitleConformational Adaptability and Thermostability in α/β-Peptide Fibrils Induced by β-Amino Acid Substitution.
Journal, issue, pagesNano Lett, Year 2025
Publish dateDec 20, 2025
AuthorsYingshan Li / Danni Li / Yuxuan Yao / Kaien Liu / Qinyue Zhao / Yiling Zhang / Yongyi Xu / Dan Li / Bo Sun / Cong Liu / Bin Dai /
PubMed AbstractThe self-assembly of peptides into amyloid fibrils enables the design of functional biomaterials, yet the conformational constraints of α-peptides limit the attainable supramolecular diversity. ...The self-assembly of peptides into amyloid fibrils enables the design of functional biomaterials, yet the conformational constraints of α-peptides limit the attainable supramolecular diversity. Here, we introduce β-amino acids, β-phenylalanine (β-Phe), and β-homophenylalanine (β-hPhe) into the reversible fibril-forming core sequence hnRAC1 to generate α/β-peptide variants with distinct architectures and enhanced thermal stability. Cryo-EM reveals that β-modified peptides assemble into polymorphic fibrils with cross-β structures that differ markedly from each other and from native hnRAC1. Comparative structural analysis indicates that backbone extension by β-residues increases subunit conformational heterogeneity, enabling tighter packing and formation of more thermostable fibrils. Examination of intra- and intermolecular contacts shows that enhanced π-π 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.
External linksNano Lett / PubMed:41420871
MethodsEM (helical sym.)
Resolution2.58 - 3.38 Å
Structure data

65211

9vnk

EMDB-65211, PDB-9vnk:
Cryo-EM structure of hnRAC1-2,8beta fibril polymorph2
Method: EM (helical sym.) / Resolution: 3.38 Å

65213

9vnm

EMDB-65213, PDB-9vnm:
Cryo-EM structure of hnRAC1-2,8beta fibril polymorph1
Method: EM (helical sym.) / Resolution: 3.37 Å

65214

9vnn

EMDB-65214, PDB-9vnn:
Cryo-EM structure of hnRAC1-2,8homobeta fibril
Method: EM (helical sym.) / Resolution: 2.58 Å

Source
  • homo sapiens (human)
KeywordsPROTEIN FIBRIL / beta amino acid modified peptide

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