The eugenol functionalized B12N12 and B16N16 cages as potential inhibitors of TNF-α and HER2 receptors

Abstract

This study aimed to explore the potential of eugenol, B12N12, B16N16, and their complexes against TNF-α (PDB ID: 2AZ5) and HER2 (PDB ID: 3RCD) proteins using Density Functional Theory (DFT) methods, focusing on their spectroscopic, electronic, and thermodynamic parameters as well as the docking of the structures. DFT calculations using the PBE1PBE-D3/6–31 + G** method was performed on the studied structures for geometry optimization, energy calculations, Mulliken population analysis, density of states (DOS), molecular electrostatic potential (MEP), frontier orbital molecules, and UV–Vis and IR spectroscopies. Analysis of the parameters revealed that the adsorption of eugenol via its methoxy group (complexes A and C) over B12N12 and B16N16 cages had the largest negative binding energies, with Ead of –23.09 and −20.49 kcal/mol, respectively. The enthalpy (ΔH) and free energy (ΔG) values for complex A were –23.20 and −9.27 kcal/mol, while for complex C they were −20.54 and −6.79 kcal/mol. The negative values of these parameters indicate that the adsorption process on the cages was exothermic. The quantum molecular descriptor values, alteration of UV–Vis peaks, and IR spectra of the complexes showed higher reactivity compared to pure eugenol. Molecular docking showed that the interaction of eugenol via its methoxy group on the B16N16 cage (complex C) had the best binding affinity and inhibition potential for TNF-α and HER2 in comparison with pure eugenol. The complex had a lower free binding energy value of −5.68 kcal/mol (with TNF-α receptor) and −5.43 kcal/mol (with HER2) compared to pure eugenol, which has energy values of −4.31 and −4.64 kcal/mol, respectively. These findings indicated that the eugenol/B16N16 compound (complex C) is a promising preventive agent against inflammatory diseases and breast cancer.