Influence of BSA on micelle formation of SDBS and CPC: An experimental–theoretical approach of its binding properties

Serum albumins play important roles in many physiological functions and serve as transporters in the transportation and distribution of endogenous and exogenous substances. Ligand-protein interaction experiments and computational approach have great significance in gaining fundamental binding characteristic of the complex. This work reports the interactions of Bovine serum albumin (BSA) with Sodium dodecyl benzene sulfonate (SDBS) and Cetyl pyridinium chloride (CPC), that have been measured by electrical conductivity, spectrophotometric and computational studies. Micellization of ionic surfactants is delayed by concentration of BSA and the temperature also restricted the same. Binding efficiency of BSA to that of ionic surfactants has been determined by absorbance spectroscopy. Computational studies confirmed the presence of 8 binding sites of BSA for SDBS and CPC. It was found that the low energy binding sites of BSA were more preferred by ionic surfactants.