Insights into the Hierarchical Assembly of a Chemically Diverse Peptide Hydrogel Derived from Human Semenogelin I.

ABSTRACT: A peptide corresponding to a 13-residue segment of the human protein semenogelin I has been shown to generate a hydrogel consisting of amyloid-like fibrils. The relative chemical diversity (compared to synthetic de novo sequences) with 11 distinct amino acids makes this peptide (P0) an ideal candidate for investigating the role of individual residues in gelation. Herein, the N-terminal residues have been sequentially removed to furnish a series of truncated peptides, P1-P10, ranging from 12 to 3 residues in length. FTIR spectroscopy investigations reveal that P0-P6 forms a β-sheet secondary structure while shorter sequences do not self-assemble. Site-specific isotope labeling of the amide backbone of P0-P2 with the IR-sensitive vibrational probe ¹³C═O yields FTIR s

SUBMITTER: Pogostin BH 

PROVIDER: S-EPMC11562788 | biostudies-literature | 2024 Nov

REPOSITORIES: biostudies-literature