Structural effects of the antimicrobial peptide maculatin 1.1 on supported lipid bilayers

David I Fernandez, Anton P Le Brun, Tzong-Hsien Lee, Paramjit S Bansal, Marie-Isabel Aguilar, Michael James, Frances Separovic

Research output: Contribution to journalArticleResearchpeer-review

41 Citations (Scopus)

Abstract

The interactions of the antimicrobial peptide maculatin 1.1 (GLFGVLAKVAAHVVPAIAEHF-NH(2)) with model phospholipid membranes were studied by use of dual polarisation interferometry and neutron reflectometry and dimyristoylphosphatidylcholine (DMPC) and mixed DMPC-dimyristoylphosphatidylglycerol (DMPG)-supported lipid bilayers chosen to mimic eukaryotic and prokaryotic membranes, respectively. In DMPC bilayers concentration-dependent binding and increasing perturbation of bilayer order by maculatin were observed. By contrast, in mixed DMPC-DMPG bilayers, maculatin interacted more strongly and in a concentration-dependent manner with retention of bilayer lipid order and structure, consistent with pore formation. These results emphasise the importance of membrane charge in mediating antimicrobial peptide activity and emphasise the importance of using complementary methods of analysis in probing the mode of action of antimicrobial peptides.
Original languageEnglish
Pages (from-to)47 - 59
Number of pages13
JournalEuropean Biophysics Journal
Volume42
Issue number1
DOIs
Publication statusPublished - 2013

Cite this