Surface plasmon resonance spectroscopy: An emerging tool for the study of peptide–membrane interactions

Abstract

The interactions between peptides and membranes mediate a wide variety of biological processes, and characterization of the molecular details of these interactions is central to our understanding of cellular events such as protein trafficking, cellular signaling and ion‐channel formation. A wide variety of biophysical techniques have been combined with the use of model membrane systems to study peptide–membrane interactions, and have provided important information on the relationship between membrane‐active peptide structure and their biological function. However, what has generally not been reported is a detailed analysis of the affinity of peptide for different membrane systems, which has largely been due to the difficulty in obtaining this information. To address this issue, surface plasmon resonance (SPR) spectroscopy has recently been applied to the study of biomembrane‐based systems using both planar mono‐ or bilayers or liposomes. This article provides an overview of these recent applications that demonstrate the potential of SPR to enhance our molecular understanding of membrane‐mediated peptide function. © 2002 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 66: 3–18, 2002