The Mechanisms of Lipid-Mediated Regulation of the Activity of Antimicrobial Peptides of Different Secondary Structure

The present study focuses on the membrane activity of antimicrobial peptides different secondary structure: bactenecin, an peptide, which forms a loop stabilized by single disulfide bond; defensins, beta-sheet structure that are three bonds; and pediocin, lantibiotic with combined structure, including both alpha-helix regions. It has been found bactenecin ion-permeable nanopores various conductance in lipid bilayers composed phosphocholine (PC) phosphoglycerol (PG) independently saturation their hydrocarbon chains. Defensins HNP-1 HNP-2 form transmembrane pores planar membranes made from PC PG unsaturated tails. investigation ability pediocin to induce composition indicates key role PGs, while is not indispensable. Replacement for phosphoserine or cardiolipin leads loss pore-forming all tested peptides. specific interaction target cells proposed. was supported RSF (#19-14-00110).