Bulletin of the Korean Chemical Society

Korean Chemical Society (대한화학회)
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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)
  • Received : 2011.09.23
  • Accepted : 2011.11.28
  • Published : 2012.02.20
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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.

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