Abstract
Herein, we have investigated the interaction of bovine serum albumin (BSA), the most abundant globular protein, with a conventional cationic surfactant, cetyldimethylethylammonium bromide (CDMEAB), through a conductivity technique in the absence/presence of electrolyte solutions at various temperatures (298.15-323.15 K). The interaction of the protein with drugs/surfactants and other additives plays a crucial role in the body. Hence, the main concern of the study is to extract the impact of BSA on surfactant molecules and
. From the specific conductivity
concentration of surfactant plots, three different noticeable critical micelle concentration (
*) values were obtained for pure CDMEAB and its mixture with protein/protein + salts. The presence of BSA and electrolytes altered the
* values of CDMEAB revealing interactions among the studied constituents where the salt solutions reduced the
* values and created a convenient environment for favorable micellization. The negative magnitudes achieved for standard free energy changes (Δ
) suggest spontaneity of micellization while the values of Δ
and Δ
signified the existence of some electrostatic and hydrophobic interactions. The values of molar heat capacity (Δ
) were positive as well as small which was an indication of less structural deformation. Molecular Dynamics (MD) simulation for all atoms revealed that the salt ions promoted non-covalent interaction between BSA and CDMEAB, and such interactions were not observed in the absence of the salt. Protein structure remained nearly same in spite of strong interaction with CDMEAB as evident from the overall RMSD (root-mean-square deviation) values of the alpha carbons and backbone of the protein and RMSF (root-mean-square fluctuation) values of the amino acid residues present in BSA. In this work thermodynamic parameters of transfer (such as Δ
, Δ
, and Δ
) were also evaluated and the results are discussed in detail. Besides, contributions of enthalpy and entropy to free energy changes were also analyzed.