Theoretical Characterization of Schiff Base Derivative and Molecular Docking Studies with Diabetic Target Enzyme Aldose Reductase

Abstract

In this study, theoretical calculations were carried out on a Schiff base derivative molecule named 6,6'-((1E,1'E)-(pyridin-2,6-diylbis(azanyelidene))bis(metanyelylidene))bis(2-methoxyphenol) (EPBM). In order to investigate the electronic, optical and structural properties of the molecule in detail, optimization processes were carried out using B3LYP, B3PW91 methods and 6-31G(d,p) basis set within the scope of DFT. As a result of the calculations; natural bond orbital (NBO) analysis, molecular electrostatic potential surface (MEP) mapping, nonlinear optical (NLO) properties, HOMO–LUMO energy levels, optimized molecular geometry and Mulliken atomic charge distribution of the molecule were obtained in detail. Molecular docking analyses were performed with aldose reductase enzyme to evaluate the biological activity of the molecule. Molecular docking studies revealed that the EPBM compound exhibited binding energies of -9.83 and -9.90 kcal/mol with the enzymes PDB ID: 1IEI and PDB ID: 1US0, respectively. Furthermore, ADME analysis was used to investigate the effects of the molecule on lipophilicity. The results demonstrate that the EPBM compound possesses both theoretical and biologically significant properties, providing an important basis for future experimental studies aimed at the treatment of diabetes-related diseases.