Volume 59, Number 1, July 2002
|Page(s)||142 - 148|
|Section||Interdisciplinary physics and related areas of science and technology|
|Published online||01 June 2002|
Interactions between transmembrane proteins embedded in a lamellar phase, stabilized by steric interactions
Department of Pharmaceutical Sciences, Faculty of Pharmacy,
University of Toronto 19 Russell Street, Toronto, Ontario, M5S 2S2 Canada
2 Laboratoire d'Imagerie Paramétrique, UMR 7623 CNRS 15 rue de l'École de Médecine, 75270 Paris Cedex 06, France
3 Centre de Génétique Moléculaire, UPR 2420 CNRS - 91190 Gif-sur-Yvette, France
4 Laboratoire de Physique Statistique de l'École Normale Supérieure, UMR 8550 CNRS 24 rue Lhomond, 75231 Paris Cedex 05, France
Accepted: 11 April 2002
We have investigated the distribution of the transmembrane myelin proteolipid protein when inserted into an oil-swollen lamellar phase, stabilized by steric interactions. When the hydrophobic membrane thickness, D, is larger than the hydrophobic length of the protein, , only repulsive interactions are found between proteins. The repulsive forces are of electrostatic nature, arising from charges carried by the protein. The interaction potential between proteins, deduced from digitized freeze-fracture micrographs, is well fitted when the classical screened electrostatic model is used. When D is smaller than , an attractive force is observed in addition to the repulsive electrostatic interactions. The attractive force originates from the membranes fluctuations. The model of membrane-mediated interactions due to the membrane thermal undulations permits us to describe our results when used in combination with the electrostatic potential.
PACS: 87.15.Kg – Molecular interactions; membrane-protein interactions / 87.16.Dg – Membranes, bilayers, and vesicles
© EDP Sciences, 2002
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