Structural effects of the antimicrobial peptide maculatin 1.1 on supported lipid bilayers
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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.
KeywordsAntimicrobial peptide Model membranes Peptide–lipid interaction Dual polarisation interferometry Neutron reflectometry
MIA and FS thank the Australian Research Council (ARC) for financial support. FS would like to acknowledge the Australian Institute for Nuclear Science and Engineering (AINSE) (proposal ID: P1139) for their support and funding enabling this research. DIF thanks the Australian government for an Australian Postgraduate Award. We would like to thank Associate Professor Lisa Martin and Ms Stefania Piantavigna (Monash University) for their assistance with QCM-D. APLB acknowledges the Australian Nuclear Science and Technology Organisation (ANSTO) executive for funding.
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