Peptide-induced domain formation in supported lipid bilayers: direct evidence by combined atomic force and polarized total internal reflection fluorescence microscopy

Biophys J. 2010 Mar 3;98(5):815-23. doi: 10.1016/j.bpj.2009.12.4327.

Abstract

Direct visualization of the mechanism(s) by which peptides induce localized changes to the structure of membranes has high potential for enabling understanding of the structure-function relationship in antimicrobial and cell-penetrating peptides. We have applied a combined imaging strategy to track the interaction of a model antimicrobial peptide, PFWRIRIRR-amide, with bacterial membrane-mimetic supported phospholipid bilayers comprised of POPE/TOCL. Our in situ studies revealed rapid reorganization of the POPE/TOCL membrane into localized TOCL-rich domains with a concomitant change in the organization of the membranes themselves, as reflected by changes in fluorescent-membrane-probe order parameter, upon introduction of the peptide.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Absorption
  • Animals
  • Cattle
  • Fluorescent Dyes / chemistry
  • Lipid Bilayers / metabolism*
  • Lipids / chemistry
  • Membrane Microdomains / drug effects*
  • Microscopy, Atomic Force / methods*
  • Microscopy, Fluorescence / methods*
  • Peptides / pharmacology*
  • Time Factors

Substances

  • Fluorescent Dyes
  • Lipid Bilayers
  • Lipids
  • Peptides