Self-Assembly of Insulin-Derived Chimeric Peptides into Two-Component Amyloid Fibrils: The Role of Coulombic Interactions.

ABSTRACT: Canonical amyloid fibrils are composed of covalently identical polypeptide chains. Here, we employ kinetic assays, atomic force microscopy, infrared spectroscopy, circular dichroism, and molecular dynamics simulations to study fibrillization patterns of two chimeric peptides, ACC_1-13E₈ and ACC_1-13K₈, in which a potent amyloidogenic stretch derived from the N-terminal segment of the insulin A-chain (ACC_1-13) is coupled to octaglutamate or octalysine segments, respectively. While large electric charges prevent aggregation of either peptide at neutral pH, stoichiometric mixing of ACC_1-13E₈ and ACC_1-13K₈ triggers rapid self-assembly of two-component fibrils driven by favorable Coulombic interacti

SUBMITTER: Fortunka M 

PROVIDER: S-EPMC10405213 | biostudies-literature | 2023 Aug

REPOSITORIES: biostudies-literature