Interaction between bovine serum albumin and equimolarly mixed cationic-anionic surfactants decyltriethylammonium bromide-sodium decyl sulfonate.

The interactions of bovine serum albumin (BSA) with the anionic surfactant sodium decylsulfonate (C10SO3), the cationic surfactant decyltriethylammonium bromide (C10NE) and equimolarly mixed cationic-anionic surfactants C10NE-C10SO3 were investigated by surface tension, viscosity, dynamic light scattering (DLS) and circular dichroism (CD). It was shown that the single ionic surfactant C10SO3 or C10NE has obvious interaction with BSA. The presence of C10SO3 or C10NE modified BSA structure.

Surfactant-induced refolding of lysozyme.

The surfactant-lysozyme interaction was investigated by circular dichroism, fluorescence, UV, dynamic light scattering, surface tension, turbidity measurements and lysozyme activity assay. A new way of refolding of lysozyme was found. It was shown that the lysozyme unfolded by anionic surfactants could be renatured by adding cationic surfactants.