The antimicrobial peptide aurein 1.2 disrupts model membranes via the carpet mechanismElectronic supplementary information (ESI) available: Table of nSLD results from the NR in H2O and CM4 contrasts and a figure of an nSLD illustrating how the thickness from each layer is derived. See DOI: 10.1039/c2cp43099a

• Main Authors: Fernandez, David I, Le Brun, Anton P, Whitwell, Thomas C, Sani, Marc-Antoine, James, Michael, Separovic, Frances
• Format: Journal Article
• Language: English
• Published: 31.10.2012
• ISSN: 1463-9076; 1463-9084
• DOI: 10.1039/c2cp43099a

The membrane interactions of the antimicrobial peptide aurein 1.2 were studied using a range of biophysical techniques to determine the location and the mechanism of action in DMPC (dimyristoylphosphatidylcholine) and DMPC/DMPG (dimyristoylphosphatidylglycerol) model membranes that mimic characteristics of eukaryotic and prokaryotic membranes, respectively. Neutron reflectometry and solid-state NMR revealed subtle changes in membrane structure caused by the peptide. Quartz crystal microbalance with dissipation, vesicle dye leakage and atomic force microscopy measurements were used to investigate the global mode of peptide interaction. Aurein 1.2 displayed an enhanced interaction with the anionic DMPC/DMPG membrane while exhibiting primarily a surface interaction with both types of model membranes, which led to bilayer disruption and membrane lysis. The antimicrobial peptide interaction is consistent with the carpet mechanism for aurein 1.2 with discrete structural changes depending on the type of phospholipid membrane. Location and mechanism of the antimicrobial peptide aurein 1.2 in biomimetic membranes was determined using neutron reflectometry and solid-state NMR.