Antimicrobial peptide activity in asymmetric bacterial membrane mimics. (17th September 2021)

• Record Type: Journal Article
• Authors: Marx, Lisa; Frewein, Moritz P. K.; Semeraro, Enrico F.; Rechberger, Gerald N.; Lohner, Karl; Porcar, Lionel; Pabst, Georg
• Is Part Of: Faraday discussions. Volume 232(2021)
• Page Start: 435
• Page End: 447
• Publication Date: 2021-09-17
• Subjects: Chemistry -- Periodicals; Metallurgy -- Periodicals; Electrochemistry -- Periodicals; 540
• DOI: 10.1039/d1fd00039j
• Languages: English
• ISSNs: 1359-6640

Abstract

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. 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.