Interactions of the antimicrobial beta-peptide beta-17 with phospholipid vesicles differ from membrane interactions of magainins

Eur J Biochem. 2003 Mar;270(6):1240-8. doi: 10.1046/j.1432-1033.2003.03484.x.

Abstract

We have studied the interaction of beta-17, a potent synthetic antimicrobial beta-peptide, with phospholipids. We find that unlike other antimicrobial peptides such as magainin II, beta-17 facilitates the formation of nonbilayer phases, indicating that the peptide promotes negative curvature. Studies of liposomal leakage also indicate a different mode of membrane interaction relative to magainin II, but both leakage and membrane binding show that beta-17, like magainin II, has strong affinity for membranes containing anionic lipids. This is likely to be an important factor contributing to the antimicrobial specificity of the beta-peptide.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Anti-Bacterial Agents / chemistry*
  • Anti-Bacterial Agents / metabolism
  • Anti-Infective Agents / chemistry*
  • Anti-Infective Agents / metabolism
  • Antimicrobial Cationic Peptides / chemistry*
  • Antimicrobial Cationic Peptides / metabolism
  • Calorimetry, Differential Scanning
  • Cell Membrane / chemistry*
  • Cell Membrane / metabolism
  • Circular Dichroism
  • Humans
  • Lipid Bilayers / chemistry
  • Lipid Bilayers / metabolism
  • Molecular Structure
  • Phospholipids / chemistry*
  • Phospholipids / metabolism
  • Protein Binding

Substances

  • Anti-Bacterial Agents
  • Anti-Infective Agents
  • Antimicrobial Cationic Peptides
  • Lipid Bilayers
  • Phospholipids