Probing The Binding Interaction Of Zinc (Ii) Schiff Bases With Bovine Serum Albumin: A Spectroscopic And Molecular Docking Study

Entrapping of potent Schiff base with biomimetic environment using fluorescence properties enables better understanding of their interaction for drug-based application. A detailed photophysical study of zinc (II) Schiff bases, 2,6-bis((E)-((2-(dimethylamino) ethyl)imino)methyl)-4-R-phenol, where R = methyl/tertiary butyl/chloro is reported by utilizing bovine serum albumin (BSA) as the bio membrane. Steady state absorption and emission studies of Schiff base-protein system have been found to get altered by change in the compartmental ligand. Alternation of polarity caused by such compartmental ligands is reported by comparing the fluorescence behavior of the probes in microheterogeneous environment in a mixture of dioxane and water of varying composition. Hildebrand equation accounts for negative binding constants among BSA with Schiff base with Cl (-I) group as the compartmental ligand in contrast to the positive magnitudes with ligands exhibiting +I effect. Functionality of such compartmental ligands (intra interactions studied using Hirshfeld analyses) upon binding with the protein is also studied in terms of quenching and denaturation studies. Schiff base with Me is found to be the most favorable ligand that bound to BSA as corroborated from the binding, quenching, micropolarity, and docking studies. Molecular docking studies predict the affinity energies for suitable binding conformations to be similar to - 6 kcal mol(-1) for BSA-Schiff base (with Me ligand).