Aggregation behavior, interaction forces and physico-chemical parameters of cetyltrimethylammonium chloride in aqueous solution of bovine serum albumin: Impacts of short-chain alcohols and temperature.

To better understand the molecular interactions between cetyltrimethylammonium chloride (CTAC) and bovine serum albumin (BSA), we report the alteration of the physicochemical characteristics of CTAC in aqueous BSA solutions in the presence of different alcohols. The analyses were performed using the conductivity method at temperatures ranging from 298.15 to 323.15 K, with 5 K intervals. The critical micelle concentration (CMC) values of the BSA + CTAC systems were found to change with variations in alcohol type, solvent composition, and temperature. The CMC values grew with the rising alcohol content. The negative free energy changes (∆Gm0) indicated the spontaneous association of the systems in all solvents media. The magnitudes of ∆Hm0 and ∆Sm0, determined from the micellization of the systems, indicated the presence of electrostatic, ion-dipole, and hydrophobic forces. The thermodynamics of transfer (free energy ((∆Gm,tr0), enthalpy (∆Hm,tr0), entropy (∆Sm,tr0)), and compensation parameters (∆Hm0,∗ and Tc)-were also calculated, providing significant insights into the potential interactions between CTAC and BSA in the presence of various alcohol additives. Furthermore, molecular docking studies suggested the binding of CTAC to different BSA binding sites with varying affinities.