A physicochemical and conformational study of co-solvent effect on the molecular interactions between similarly charged protein surfactant (BSA-SDBS) system

Abstract

Use of surfactants in numerous household and industrial processes and their interaction with proteins in our day to day life has made protein-surfactant interactions a booming topic among the researchers of current era. Bovine serum albumin (BSA) being structural homologue to Human Serum albumin (HSA) allowed us to study its binding efficiency with anionic surfactant such as sodium dodecyl benzene sulfonate (SDBS). BSA is known as transport protein due its binding characteristics as well as transportation of hydrophobic drugs or ligands to different target areas (In Human body). Surfactants are also known as eminent constituents of pharmaceutical drug delivery systems. So, interactions of BSA-SDBS (Similarly charged protein-surfactant system) in presence of two industrially important co-solvents DMSO and Glycerol have decided its fate as a novel drug delivery system. These interactional studies were performed by means of myriad experimental and theoretical approaches i.e. conductivity, fluorescence, Ligand Simultaneous Docking (MLSD) and non-covalent interactions index (NCI). Results showed the dominance of Van der Waals interactions and hydrophobic forces with important changes in the preferred binding site.