Portal de Periódicos da CAPES

The interaction of antimicrobial peptide LL-37 with artificial biomembranes: epifluorescence and impedance spectroscopy approach

2004; IOP Publishing; Volume: 16; Issue: 26 Linguagem: Inglês

10.1088/0953-8984/16/26/014

1361-648X

Frances Neville, Marjolaine Cahuzac, Andrew Nelson, David Gidalevitz,

Biochemical and Structural Characterization

Membrane interactions of the human antimicrobial peptide LL-37 have been studied by a variety of techniques including insertion assay, epifluorescence microscopy and impedance spectroscopy. This study makes use of lipid monolayers at the air–aqueous interface to mimic bacterial or eukaryotic membranes. It was found that LL-37 readily inserts into phosphatidylglycerol (PG) and lipid A monolayers, significantly disrupting their structure. In contrast, the structure of phosphatidylcholine (PC) monolayers remains virtually unaffected by LL-37, which is evident both from epifluorescence and electrochemical measurements. Impedance spectroscopy showed that the LL-37 rich PC monolayer remains an ideal capacitor while LL-37 enriched lipid A capacitance decreases significantly, suggesting an increase in layer thickness from peptide–lipid binding.