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Lipid perturbation by membrane proteins and the lipophobic effect.

Authors
  • Duneau, Jean-Pierre1
  • Khao, Jonathan2
  • Sturgis, James N3
  • 1 Laboratoire d'Ingénierie des Systèmes Macromoléculaires, UMR 7255, CNRS and Aix-Marseille Univ, Marseille 13402 cedex 20, France. Electronic address: [email protected] , (France)
  • 2 Laboratoire d'Ingénierie des Systèmes Macromoléculaires, UMR 7255, CNRS and Aix-Marseille Univ, Marseille 13402 cedex 20, France. , (France)
  • 3 Laboratoire d'Ingénierie des Systèmes Macromoléculaires, UMR 7255, CNRS and Aix-Marseille Univ, Marseille 13402 cedex 20, France. Electronic address: [email protected] , (France)
Type
Published Article
Journal
Biochimica et Biophysica Acta (BBA) - Biomembranes
Publisher
Elsevier
Publication Date
Jan 01, 2017
Volume
1859
Issue
1
Pages
126–134
Identifiers
DOI: 10.1016/j.bbamem.2016.10.014
PMID: 27794424
Source
Medline
Keywords
Language
English
License
Unknown

Abstract

Understanding how membrane proteins interact with their environment is fundamental to the understanding of their structure, function and interactions. We have performed coarse-grained molecular dynamics simulations on a series of membrane proteins in a membrane environment to examine the perturbations of the lipids by the presence of protein. We analyze these perturbations in terms of elastic membrane deformations and local lipid protein interactions. However these two factors are insufficient to describe the variety of effects that we observe and the changes caused by membranes proteins to the structure and dynamics of their lipid environment. Other factors that change the conformation available to lipid molecules are evident and are able to modify lipid structure far from the protein surface, and thus mediate long-range interactions between membrane proteins. We suggest that these multiple modifications to lipid behavior are responsible, at the molecular level, for the lipophobic effect we have proposed to account for our observations of membrane protein organization. Copyright © 2016 Elsevier B.V. All rights reserved.

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