Structure-efficiency relationships of zwitterionic detergents as protein solubilizers in two-dimensional electrophoresis.

Several zwitterionic detergents differing in their polar heads, linker parts and hydrophobia tail were synthesized and evaluated for their efficiency in protein solubilizers for two-dimensional electrophoresis. A model system consisting of human red blood cell ghosts was used for this purpose. This study leads to the description of several new efficient detergents and allowed us to derive structural constraints for the design and synthesis of efficient detergents for two-dimensional electrophoresis. These constraints apply to the hydrophilic head (sulfobetaine but not carboxybetaine), to the hydrophobic tail (12 to 16 alkyl carbons long, linear alkyl or alkylaryl) and to the presence and nature of the linker between the hydrophilic head and hydrophobic tail.