Amyloidogenicity and lipid interaction of antimicrobial anuran peptides
2019-09-11T01:34:46Z (GMT) by
Uperin 3.x antimicrobial peptides, which can also form amyloid-like fibrils, are appropriate to study the effect of salt concentration and cationic to hydrophobic residue substitution on fibril-forming propensity of antimicrobial peptides. Sodium chloride promotes uperin 3.5 aggregation by screening electrostatic repulsion, and initially facilitating increased alpha-helical content. Uperin 3.x peptides and seventh-position alanine variants interacted more favourably with dodecyl phosphatidylcholine micelles than with sodium dodecyl sulphate micelles, with interaction of wild-type peptides being stronger. Alanine substitution increases aggregation propensity of uperin 3.x peptides. Peptide aggregates solely composed of coil and turn structures demonstrated relatively rapid beta-aggregation than other aggregates.