Aggregation Capacity and Complexation Properties of a System Based on an Imidazole-Containing Amphiphile and Bovine Serum Albumin

Abstract

A complex of physicochemical methods was used to study the aggregation characteristics of an imidazolium-containing amphiphile and its ability for complex formation with bovine serum albumin (BSA). Tensiometry showed that adding BSA to the surfactant decreases the aggregation threshold of the system by a factor of 50. Dynamic light scattering established, that the size of the surfactant–BSA complexes depends on the size of the polypeptide (6–10 nm) and is independent on the concentrations of the surfactant and BSA. The Stern‒Volmer constants and surfactant‒protein binding constants were calculated from fluorescence spectroscopy data.