Experimental and Computational Characterization of the Molecular Interaction between Bovine Serum Albumin and an Ester-functionalized Cationic Gemini Surfactant

In view of the recent emergence of surfactants as therapeutic agents for industrial-based pharmacology, the current study highlights the critical aspects of a cationic C-12-E2O2-C-12 gemini surfactant, such as pharmacodynamics and pharmacokinetics. Surface tension, fluorescence and absorption studies reveal that the gemini surfactant interacts efficiently with the BSA. The Stern-Volmer and Benesi-Hildebrand equations, utilized to compute the binding constants (K-SV and K-b), evaluated at three temperatures by utilizing fluorescence quenching data, provide evidence of static quenching and the evaluated thermodynamic parameters (which are all negative) suggest a spontaneous complexation with the pivotal role being played by both van der Waals forces and hydrogen bonds. Other complementary methods (3-D, synchronous, RRS, CD, FT-IR) confirmed conformational alterations in BSA due to the interaction. Binding of the C-12-E2O2-C-12 gemini surfactant within the protein's site I (sub-domain IIA) had been derived from site probe and molecular docking analyses. Also, the HOMO-LUMO energies, band gap energy and global reactivity descriptors of C-12-E2O2-C-12 gemini surfactant and the aromatic residues of BSA were evaluated. The study might help use C-12-E2O2-C-12, gemini surfactant as a therapeutic agent in the pharmaceutical industry.