Antimicrobial Peptides Share a Common Interaction Driven by Membrane Line Tension Reduction.

ABSTRACT: Antimicrobial peptides (AMPs) are a class of host-defense molecules that neutralize a broad range of pathogens. Their membrane-permeabilizing behavior has been commonly attributed to the formation of pores; however, with the continuing discovery of AMPs, many are uncharacterized and their exact mechanism remains unknown. Using atomic force microscopy, we previously characterized the disruption of model membranes by protegrin-1 (PG-1), a cationic AMP from pig leukocytes. When incubated with zwitterionic membranes of dimyristoylphosphocholine, PG-1 first induced edge instability at low concentrations, then porous defects at intermediate concentrations, and finally worm-like micelle structures at high concentrations. These rich structural changes suggested that pore formation constitutes only

SUBMITTER: Henderson JM 

PROVIDER: S-EPMC5113125 | biostudies-literature | 2016 Nov

REPOSITORIES: biostudies-literature