The interaction of antimicrobial peptide LL-37 with artificial biomembranes: epifluorescence and impedance spectroscopy approach
Year: 2004
Type: article
Abstract: 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.
Institutions: University of Leeds, Illinois Institute of Technology
Language: English
Subfield: Microbiology
Field: Immunology and Microbiology
Domain: Life Sciences
Open Access status: bronze
OpenAlex ID: W2002246578