Association of bovine serum albumin and cetyltrimethylammonium chloride: An investigation of the effects of temperature and hydrotropes

Abstract

Interactions between bovine serum albumin (BSA) and cetyltrimethylammonium chloride (CTAC) were studied utilizing conductivity approach. The critical micelle concentration (CMC), micelle ionization (α) along with counter ion binding (β) of CTAC micellization in aqueous solutions of BSA/BSA + hydrotropes (HYTs) have been computed at 298.15−323.15 K. Increase in temperatures of CTAC + BSA/BSA mixtures in HYTs resulted in elevation of CMC due to the association of chemical species in the respective systems which reduced the degree of micelle formation. CTAC + BSA consumed greater extents of surfactant species to generate micelle formation in the corresponding systems at higher temperatures. Standard free energy change ∆Gm0 associated with the assembling processes of CTAC in BSA was found negative suggesting the spontaneous nature of micellization processes. Magnitudes of ∆Hm0 and ∆Sm0 obtained from CTAC + BSA aggregation revealed the existence of H-bonding, electrostatic interactions along with hydrophobic forces among the constituents employed in the respective systems. ∆Gm0 The estimated thermodynamic parameters of transfer (free energy (∆Gm,tr0), enthalpy (∆Hm,tr0) and entropy (∆Sm,tr0)) and compensation variables (∆Hm0,∗ and Tc) provided significant insights on the association behaviors of the CTAC + BSA system in the selected HYTs solutions.