Abstract
Interaction of fusogenic or membrane-perturbing peptides with lipid bilayers often involves drastic rearrangements of the membrane structure, with redistribution of lipids, inducement of bilayer curvature, or formation of nonbilayer or multibilayer structures. Fluorescence (or Forster) Resonance Energy Transfer (FRET) is a photophysical technique which has an acute sensitivity to distances in the nanometer range, and, as such, is particularly suited to probe alterations in membrane organization in this length scale. This article reviews methods and selected applications of FRET in this field, from the now classic (fusion induced) lipid-mixing assay to examples where kinetic modeling of FRET enables the recovery of topological information.
Keywords: Fluorescence, FRET, Lipid demixing, Lipid-peptide interaction, Membrane fusion
Protein & Peptide Letters
Title: Characterization of Peptide-Induced Morphological Alterations in Membranes by Fluorescence Resonance Energy Transfer
Volume: 16 Issue: 7
Author(s): Luis M.S. Loura and Manuel Prieto
Affiliation:
Keywords: Fluorescence, FRET, Lipid demixing, Lipid-peptide interaction, Membrane fusion
Abstract: Interaction of fusogenic or membrane-perturbing peptides with lipid bilayers often involves drastic rearrangements of the membrane structure, with redistribution of lipids, inducement of bilayer curvature, or formation of nonbilayer or multibilayer structures. Fluorescence (or Forster) Resonance Energy Transfer (FRET) is a photophysical technique which has an acute sensitivity to distances in the nanometer range, and, as such, is particularly suited to probe alterations in membrane organization in this length scale. This article reviews methods and selected applications of FRET in this field, from the now classic (fusion induced) lipid-mixing assay to examples where kinetic modeling of FRET enables the recovery of topological information.
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Cite this article as:
Loura M.S. Luis and Prieto Manuel, Characterization of Peptide-Induced Morphological Alterations in Membranes by Fluorescence Resonance Energy Transfer, Protein & Peptide Letters 2009; 16 (7) . https://dx.doi.org/10.2174/092986609788681698
DOI https://dx.doi.org/10.2174/092986609788681698 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |

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