4.5 Review

Membrane lipid phase transitions and phase organization studied by Fourier transform infrared spectroscopy

Journal

BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES
Volume 1828, Issue 10, Pages 2347-2358

Publisher

ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbamem.2012.10.018

Keywords

Fourier transform infrared spectroscopy; Phospholipids; Lipid bilayers; Lipid phase transitions; Phase structure

Funding

  1. Medical Research Council of Canada
  2. Canadian Institutes of Health Research
  3. Alberta Heritage Foundation for Medical Research

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Fourier transform infrared (FUR) spectroscopy is a powerful yet relatively inexpensive and convenient technique for studying the structure and organization of membrane lipids in their various polymorphic phases. This spectroscopic technique yields information about the conformation and dynamics of all regions of the lipid molecule simultaneously without the necessity of introducing extrinsic probes. In this review, we summarize some relatively recent FTIR spectroscopic studies of the structure and organization primarily of fully hydrated phospholipids in their biologically relevant lamellar crystalline, gel and liquid crystalline phases, and show that interconversions between these bilayer phases can be accurately monitored by this technique. We also briefly discuss how the structure and organization of potentially biologically relevant nonlamellar micellar or reversed hexagonal lipid phases can be studied and how phase transitions between lamellar and nonlamellar phases, or between various nonlamellar phases, can be followed as well. In addition, we discuss the potential for FUR spectroscopy to yield fairly high resolution structural information about phospholipid packing in lamellar crystalline or gel phases. Finally, we show that many, but not all of these FUR approaches can also yield valuable information about lipid protein interactions in membrane protein- or peptide-containing lipid membrane bilayer model or even in biological membranes. This article is part of a Special Issue entitled: FUR in membrane proteins and peptide studies. (C) 2012 Elsevier B.V. All rights reserved.

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