Abstract
Membrane interactions of the human antimicrobial peptide LL-37 have been studied by avariety of techniques including insertion assay, epifluorescence microscopy and impedancespectroscopy. This study makes use of lipid monolayers at the air–aqueous interface tomimic bacterial or eukaryotic membranes. It was found that LL-37 readily inserts intophosphatidylglycerol (PG) and lipid A monolayers, significantly disrupting their structure.In contrast, the structure of phosphatidylcholine (PC) monolayers remains virtuallyunaffected by LL-37, which is evident both from epifluorescence and electrochemicalmeasurements. Impedance spectroscopy showed that the LL-37 rich PC monolayerremains an ideal capacitor while LL-37 enriched lipid A capacitance decreasessignificantly, suggesting an increase in layer thickness from peptide–lipid binding.
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