The antimicrobial peptide aurein 1.2 disrupts model membranes via the carpet mechanism

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 characteris...

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Published inPhysical chemistry chemical physics : PCCP Vol. 14; no. 45; pp. 15739 - 15751
Main Authors FERNANDEZ, David I, LE BRUN, Anton P, WHITWELL, Thomas C, SANI, Marc-Antoine, JAMES, Michael, SEPAROVIC, Frances
Format Journal Article
LanguageEnglish
Published Cambridge Royal Society of Chemistry 05.12.2012
Subjects
Antimicrobial Cationic Peptides - chemistry
Cell Membrane - chemistry
Chemistry
Colloidal state and disperse state
Dimyristoylphosphatidylcholine - chemistry
Eukaryotic Cells - chemistry
Exact sciences and technology
General and physical chemistry
Membranes
Models, Molecular
Phosphatidylglycerols - chemistry
Prokaryotic Cells - chemistry
Vesicle
Atomic force microscopy
Dyes
Peptides
Membrane interaction
Crystals
Phospholipid
NMR spectrometry
Neutron reflection
Bilayer
Antimicrobial agent
Mechanism
Solid state
Dissipation
Membrane
Models
Structure
Quartz microbalance
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Summary: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.
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ISSN:1463-9076
1463-9084
DOI:10.1039/c2cp43099a