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

Fernandez, David I., Le Brun, Anton P., Lee, Tzong-Hsien, Bansal, Paramjit, Aguilar, Marie-Isabel, James, Michael, and Separovic, Frances (2013) Structural effects of the antimicrobial peptide maculatin 1.1 on supported lipid bilayers. European Biophysics Journal, 42 (1). pp. 47-59.

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Abstract

The interactions of the antimicrobial peptide maculatin 1.1 (GLFGVLAKVAAHVVPAIAEHF-NH2) 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.

Item ID: 26434
Item Type: Article (Research - C1)
ISSN: 1432-1017
Keywords: antimicrobial peptide, model membranes, peptide–lipid interaction, dual polarisation interferometry, neutron reflectometry
Funders: Australian Research Council (ARC), Australian Institute of Nuclear Science and Engineering (AINSE), Australian Nuclear Science and Technology Organisation (ANSTO)
Date Deposited: 08 Apr 2014 23:18
FoR Codes: 11 MEDICAL AND HEALTH SCIENCES > 1101 Medical Biochemistry and Metabolomics > 110106 Medical Biochemistry: Proteins and Peptides (incl Medical Proteomics) @ 100%
SEO Codes: 97 EXPANDING KNOWLEDGE > 970106 Expanding Knowledge in the Biological Sciences @ 100%
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