Spectroscopic Investigation of the Interaction of BSA with Cationic Surfactants

The interactions between dodecyltrimethylammonium bromide (DTAB), tetradecyltrimethylammonium bromide (TTAB), cetyltrimethylammonium bromide (CTAB), and hexadecylpyridinium chloride (HDPC) with bovine serum albumin (BSA) in an aqueous solution (pH = 7.0, 0.001 M HEPES buffer) were studied by fluorescence and circular dichroism (CD) measurements. These categories of surfactants were used to elucidate the effect of hydrophilic group and length of hydrophobic chain surfactant on the mechanism of binding to BSA. The result revealed that for all surfactants, at low concentrations, the Stern‐Volmer plots have an upward curvature and in high concentrations, the quenching efficiency was decreased with increase in surfactant concentration. The activation energy of the interaction between cationic surfactants and BSA was measured. The results of CD show that the conformation of BSA has been changed in the presence of cationic surfactants. Cationic surfactants act as denaturants and solubilizing agents for membranes of proteins and, hence, the study of protein–surfactant interactions is of great importance. Circular dichroism measurements show that the conformation of bovine serum albumin (BSA) as a model protein, changes in the presence of cationic surfactants.