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http://dx.doi.org/10.5012/bkcs.2012.33.2.426

A Solid-state NMR Study of the Kinetics of the Activity of an Antimicrobial Peptide, PG-1 on Lipid Membranes  

Kim, Chul (Department of Chemistry, Hannam University)
Wi, Sungsool (Department of Chemistry, Virginia Tech)
Publication Information
Bulletin of the Korean Chemical Society / v.33, no.2, 2012 , pp. 426-432 More about this Journal
Abstract
The activity of an antimicrobial peptide, protegrin-1 (PG-1), on lipid membranes was investigated using solidstate NMR and a new sampling method that employed mechanically aligned bilayers between thin glass plates. At 95% hydration and full hydration, the peptide respectively disrupted 25% and 86% of the aligned 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphotidylcholine (POPC) bilayers at a P/L (peptide-to-lipid) ratio of 1/20 under the new experimental conditions. The kinetics of the POPC bilayers disruption appeared to be diffusioncontrolled. The presence of cholesterol at 95% hydration and full hydration reduced the peptide disruption of the aligned POPC bilayers to less than 10% and 35%, respectively. A comparison of the equilibrium states of heterogeneously and homogeneously mixed peptides and lipids demonstrated the importance of peptide binding to the biomembrane for whole membrane disruption.
Keywords
Antimicrobial peptide; Lipid bilayer; Hydration; Cholesterol; Solid-state NMR;
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