Abstract
Membrane proteins (MPs), which correspond to about 30% of the proteome, perform a wide range of essential cellular functions and therefore have a considerable therapeutic importance. The extraction and isolation of MPs from their biological environment is a primordial step for the determination of their structures as well as a requirement for the understanding of their role and function. The recent findings have resulted from efforts undertaken in obtaining pure homogeneous membrane proteins and understanding protein-lipid and protein-detergent interactions for proper stabilization of the active form. Indeed, detergents, which are commonly used for MP extraction, can often lead to the destabilization and irreversible inactivation of MPs because of their dissociating effect. 1 To circumvent these problems, current research focuses on the development of alternative approaches to classical detergents. 2 Among these novel approaches, one can cite amphipathic peptides, 3 tripod amphiphiles, 4 tandem facial amphiphiles, 5 amphipathic polymers, 6-8 and fluorinated surfactants (FS). 9