Abstract
Solid-state NMR is a powerful tool to study the interaction between membrane-active peptides, such as antimicrobial peptides, with lipid membranes mimicking the composition and structure of cells. By exploiting the orientation and motion dependence of lipid nuclear tensors in the magnetic field, information on the peptide activity with lipid bilayers can be obtained. 31P and 2H solid-state NMR experiments probe the lipid headgroup and the acyl chain region, respectively, to investigate the peptide location and the eventual structural modification triggered by these membrane-active molecules. The effects of frog antimicrobial peptides on lipid systems mimicking eukaryotic versus prokaryotic cell membranes are presented. Static and magic angle spinning NMR techniques, including aligned samples and sideband analysis, provide valuable information on the activity and molecular mechanism by which these antimicrobial peptides disrupt lipid bilayers.
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