Alternative Causal Link between Peptide Fibrillization and β-Strand Conformation.

ABSTRACT: In the prevailing phenomenon of peptide fibrillization, β-strand conformation has long been believed to be an important structural basis for peptide assembly. According to a widely accepted theory, in most peptide fibrillization processes, peptide monomers need to intrinsically take or transform to β-strand conformation before they can undergo ordered packing to form nanofibers. In this study, we reported our findings on an alternative peptide fibrillization pathway starting from a disordered secondary structure, which could then transform to β-strand after fibrillization. By using circular dichroism, thioflavin-T binding test, and transmission electron microscopy, we studied the secondary structure and assembly behavior of Ac-RADARADARADARADA-NH₂ (RADA16-I) in a low concentrati

SUBMITTER: Xing Z 

PROVIDER: S-EPMC8154227 | biostudies-literature | 2021 May

REPOSITORIES: biostudies-literature