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

Abstract 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.