Inner field compensation as a tool for the characterization of asymmetric membranes and Peptide-membrane interactions

Biophys J. 2004 Feb;86(2):913-22. doi: 10.1016/S0006-3495(04)74167-3.

Abstract

Symmetric and asymmetric planar lipid bilayers prepared according to the Montal-Mueller method are a powerful tool to characterize peptide-membrane interactions. Several electrical properties of lipid bilayers such as membrane current, membrane capacitance, and the inner membrane potential differences and their changes can be deduced. The time-resolved determination of peptide-induced changes in membrane capacitance and inner membrane potential difference are of high importance for the characterization of peptide-membrane interactions. Intercalation and accumulation of peptides lead to changes in membrane capacitance, and membrane interaction of charged peptides induces changes in the charge distribution within the membrane and with that to changes in the membrane potential profile. In this study, we establish time-resolved measurements of the capacitance minimization potential DeltaPsi on various asymmetric planar lipid bilayers using the inner field compensation method. The results are compared to the respective ones of inner membrane potential differences DeltaPhi determined from ion carrier transport measurements. Finally, the time courses of membrane capacitances and of DeltaPsi have been used to characterize the interaction of cathelicidins with reconstituted lipid matrices of various Gram-negative bacteria.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Antimicrobial Cationic Peptides / chemistry*
  • Cathelicidins
  • Electric Capacitance
  • Electrochemistry / methods*
  • Electromagnetic Fields
  • Lipid Bilayers / chemistry*
  • Membrane Potentials
  • Membrane Proteins / chemistry*
  • Peptides / chemistry
  • Phospholipids / chemistry*
  • Protein Binding
  • Static Electricity

Substances

  • Antimicrobial Cationic Peptides
  • Cathelicidins
  • Lipid Bilayers
  • Membrane Proteins
  • Peptides
  • Phospholipids