The instability of membrane proteins in detergent solution can generally be traced to the dissociating character of detergents and often correlates with delipidation. We examine here the possibility of substituting detergents, after membrane proteins have been solubilized, with non-detergent surfactants whose hydrophobic moiety contains a perfluorinated region that makes it lipophobic. In order to improve its affinity for the protein surface, the fluorinated chain is terminated by an ethyl group. Test proteins included bacteriorhodopsin, the cytochrome b6f complex, and the transmembrane region of the bacterial outer membrane protein OmpA. All three proteins were purified using classical detergents and transferred into solutions of C2H5C 6F12C2H4-S-poly-Tris-(hydroxymethyl) aminomethane (HF-TAC). Transfer to HF-TAC maintained the native state of the proteins and prevented their precipitation. Provided the concentration of HF-TAC was high enough, HF-TAC/membrane protein complexes ran as single bands upon centrifugation in sucrose gradients. Bacteriorhodopsin and the cytochrome b 6f complex, both of which are detergent-sensitive, exhibited increased biochemical stability upon extended storage in the presence of a high concentration of HF-TAC as compared to detergent micelles. The stabilization of cytochrome b6f is at least partly due to a better retention of protein-bound lipids. © 2004 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
Breyton, C., Chabaud, E., Chaudier, Y., Pucci, B., & Popot, J. L. (2004). Hemifluorinated surfactants: A non-dissociating environment for handling membrane proteins in aqueous solutions? In FEBS Letters (Vol. 564, pp. 312–318). https://doi.org/10.1016/S0014-5793(04)00227-3