Structure of protein–surfactant complexes as studied by small-angle neutron scattering and dynamic light scattering

Abstract

The structure of protein–surfactant complexes of bovine serum albumin (BSA) and sodium dodecyl sulfate (SDS) has been studied using small-angle neutron scattering (SANS) and dynamic light scattering (DLS). SANS data indicate that addition of BSA to micellar surfactant solution leads to the formation of a complex that has a fractal structure. The fractal structure has been evaluated using a necklace model considering that the micelle-like aggregates are randomly distributed around the polypeptide chain. We have observed that the structure of protein–surfactant complex is independent of the size of micelles in their pure surfactant solutions. The SDS micelle size was varied using salts LiBr or/and NaBr, where SDS forms larger micelles in presence of NaBr than LiBr. The fractal dimension and the extent of the complex as well as the size and number of micelles attached to the complex have been determined. The micelle-like aggregates bound to protein in the complex are spherical with a much smaller aggregation number than those in pure surfactant solutions. DLS measurements support the above results on the protein–surfactant complexes as obtained using SANS.