Abstract
Handling integral membrane proteins in aqueous solutions traditionally relies on the use of detergents, which are surfactants capable of dispersing the components of biological membranes into mixed micelles. The dissociating character of detergents, however, most often causes solubilized membrane proteins to be unstable. This has prompted the development of alternative, less-aggressive surfactants designed to keep membrane proteins soluble, after they have been solubilized, under milder conditions. A short overview is presented of the structure, properties, and uses of two families of such surfactants: amphiphilic polymers (“amphipols”) and fluorinated surfactants.
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Acknowledgments
Particular thanks are due to J.-L. Banères, L.J. Catoire, D. Charvolin, T. Dahmane, F. Giusti, Y. Gohon, F. Lebaupain, K.L. Martinez, and M. Zoonens for suggestions about the manuscript and help with the figures. Thanks are also due to A. Polidori and G. Durand, from LCBOSMV, who were greatly involved in the synthesis and physical-chemical analysis of various FSs or non-ionic APols. This work has benefited, in particular, from funding by the EC BIO4-CT98-0269; STREP LSHG-CT-2005-513770 IMPS (Innovative Tools for Membrane Protein Structural Proteomics), the Human Frontier Science Program Organization (grant RG00223/2000-M), the Agence Nationale pour la Recherche PCV07 186241, and the CNRS (Interdisciplinary program Physique et Chimie du Vivant; DRITT grant ST 83747-04).
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Breyton, C., Pucci, B., Popot, JL. (2010). Amphipols and Fluorinated Surfactants: Two Alternatives to Detergents for Studying Membrane Proteins In vitro . In: Mus-Veteau, I. (eds) Heterologous Expression of Membrane Proteins. Methods in Molecular Biology™, vol 601. Humana Press. https://doi.org/10.1007/978-1-60761-344-2_14
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