Structure and Activity of Protegiun-1 in Model Lipid Membranes

Publisher Website
Google Scholar
Abstract
Protegrin (PG)-1, an antimicrobial peptide from porcine leukocytes, mediated the release of encapsulated fluorescent dye from vesicles of simulated microbial lipids, suggesting that the peptide interacted strongly with membrane-mimetic ensembles. Circular dichroism measurements of PG-1 in membrane-lipid dispersions and liposomal systems indicated that the peptide assumed a predominantly β-sheet conformation in these environments. Fourier transform infrared measurements of the peptide in microbial lipid films showed that the P­ sheet component was oriented approximately parallel to the surface of the lipid film The ability of PG-1 to associate with and lyse model microbial-lipid membranes is likely to underlie its potent antibiotic properties.

This publication has 0 references indexed in Scilit: