Volume 232, 2021

Antimicrobial peptide activity in asymmetric bacterial membrane mimics

Abstract

We report on the response of asymmetric lipid membranes composed of palmitoyl oleoyl phosphatidylethanolamine and palmitoyl oleoyl phosphatidylglycerol, to interactions with the frog peptides L18W-PGLa and magainin 2 (MG2a), as well as the lactoferricin derivative LF11-215. In particular we determined the peptide-induced lipid flip-flop, as well as membrane partitioning of L18W-PGLa and LF11-215, and vesicle dye-leakage induced by L18W-PGLa. The ability of L18W-PGLa and MG2a to translocate through the membrane appears to correlate with the observed lipid flip-flop, which occurred at the fastest rate for L18W-PGLa. The higher structural flexibility of LF11-215 in turn allows this peptide to insert into the bilayers without detectable changes of membrane asymmetry. The increased vulnerability of asymmetric membranes to L18W-PGLa in terms of permeability, appears to be a consequence of tension differences between the compositionally distinct leaflets, but not due to increased peptide partitioning.

Graphical abstract: Antimicrobial peptide activity in asymmetric bacterial membrane mimics

Associated articles

Supplementary files

Article information

Article type
Paper
Submitted
21 Jun 2021
Accepted
21 Jul 2021
First published
21 Jul 2021
This article is Open Access
Creative Commons BY license

Faraday Discuss., 2021,232, 435-447

Antimicrobial peptide activity in asymmetric bacterial membrane mimics

L. Marx, M. P. K. Frewein, E. F. Semeraro, Gerald N. Rechberger, K. Lohner, L. Porcar and G. Pabst, Faraday Discuss., 2021, 232, 435 DOI: 10.1039/D1FD00039J

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