Self-assembly dynamics and antimicrobial activity of all l- and d-amino acid enantiomers of a designer peptide.

ABSTRACT: Recent studies have shown that antimicrobial peptides (AMPs) can self-assemble into supramolecular structures, but this has been overlooked as causative of their antimicrobial activity. Also, the higher antimicrobial potency of d-enantiomers compared to l-enantiomers of AMPs cannot always be attributed to their different resistance to protease degradation. Here, we tested all l- and d-amino acid versions of GL13K, an AMP derived from a human protein, to study structural links between the AMP secondary structure, supramolecular self-assembly dynamics, and antimicrobial activity. pH dependence and the evolution of secondary structures were related to a self-assembly process with differences among these AMPs. The two GL13K enantiomers formed analogous self-assembled twisted nanoribbon structu

SUBMITTER: Ye Z 

PROVIDER: S-EPMC6319268 | biostudies-literature | 2018 Dec

REPOSITORIES: biostudies-literature