Experimental and Computational Characterization of Oxidized and Reduced Protegrin Pores in Lipid Bilayers.

ABSTRACT: Protegrin-1 (PG-1), an 18-residue β-hairpin stabilized by two disulfide bonds, is a member of a family of powerful antimicrobial peptides which are believed to act through membrane permeabilization. Here we used a combination of experimental and computational approaches to characterize possible structural arrangements of PG-1 in lipid bilayers mimicking bacterial membranes. We have measured the dose-response function of the PG-1-induced leakage of markers of various sizes from vesicles and found it to be consistent with the formation of pores of two different sizes. The first one allows the release of small dyes and occurs at peptide:lipid ratios < 0.006. Above this ratio, larger pores are observed through which the smallest of dextrans FD4 can be released. In parallel with pore formation,

SUBMITTER: Rodnin MV 

PROVIDER: S-EPMC7360341 | biostudies-literature | 2020 Jun

REPOSITORIES: biostudies-literature