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

摘要

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 SternaEuro'Volmer constants and surfactantaEuro'protein binding constants were calculated from fluorescence spectroscopy data.