Amphipols: polymeric surfactants for membrane
biology research |
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| Authors: | J-L Popot E A Berry D Charvolin C Creuzenet C Ebel D M Engelman M Flötenmeyer F Giusti Y Gohon P Hervé Q Hong J H Lakey K Leonard H A Shuman P Timmins D E Warschawski F Zito M Zoonens B Pucci C Tribet |
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| Institution: | (1) UMR 7099, CNRS and Université Paris-7, Institut de Biologie Physico-Chimique, CNRS IFR 550, Laboratoire de Physico-Chimie Moléculaire des Membranes Biologiques, 13 rue Pierre et Marie Curie, 75005 Paris, France;(2) Lawrence Berkeley National Laboratory, 1 Cyclotron Road, 94720 Berkeley, California, USA;(3) Department of Biology and Chemistry, Massachusetts Institute of Technology, 77 Massachusetts Ave., 02139 Cambridge, Massachusetts, USA;(4) Institut de Biologie Structurale, UMR 5075 CEA-CNRS-UJF, Laboratoire de Biophysique Moléculaire, 41 rue Jules Horowitz, 38027 Grenoble, Cedex 01, France;(5) Department of Molecular Biophysics and Biochemistry, Yale University, 420 Bass Center, 06520-8114 New Haven, Connecticut, USA;(6) European Molecular Biology Laboratory, Meyerhofstrasse 1, 69117 Heidelberg, Germany;(7) University of Newcastle upon Tyne, School of Cell and Molecular Biosciences, the Medical School, NE2 4HH Newcastle, United Kingdom;(8) Department of Microbiology, Hammer Science Center, College of Physicians and Surgeons, Columbia University, 701 West 168th Street, 10032 New York, New York, USA;(9) Institut Laue-Langevin, Large Scale Structures Group, Avenue des Martyrs, B.P.156, 38042 Grenoble, Cedex 9, France;(10) Université d'Avignon, Laboratoire de Chimie Bioorganique et des Systèmes Moléculaires Vectoriels, 33 rue Louis Pasteur, 84000 Avignon, France;(11) CNRS UMR 7615, ESPCI, Laboratoire de Physico-Chimie Macromoléculaire, 10 rue Vauquelin, 75005 Paris, France;(12) Present address: Department of Microbiology and Immunology, University of Western Ontario, Dental Sciences Building, N6A 5C1 London, Canada |
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| Abstract: | Membrane proteins classically are handled in aqueous solutions as complexes with detergents. The dissociating character of detergents, combined with the need to maintain an excess of them, frequently results in more or less rapid inactivation of the protein under study. Over the past few years, we have endeavored to develop a novel family of surfactants, dubbed amphipols (APs). APs are amphiphilic polymers that bind to the transmembrane surface of the protein in a noncovalent but, in the absence of a competing surfactant, quasi-irreversible manner. Membrane proteins complexed by APs are in their native state, stable, and they remain water-soluble in the absence of detergent or free APs. An update is presented of the current knowledge about these compounds and their demonstrated or putative uses in membrane biology. |
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| Keywords: | Membrane proteins surfactants detergents amphipols |
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