Molecular Modeling and Simulation of glycine functionalized B12N12 and B16N16 nanoclusters as potential inhibitors of proinflammatory cytokines

•Glycine adsorption on BN nanoclusters are evaluated using DFT and molecular docking.•B12N12 demonstrates strong tendency towards the adsorption of amine group from the glycine molecule.•Glycine adsorption on B12N12 increases adsorption energy and dipole moment.•Molecular docking analysis showed that the Gly /B12N12 complexe has a good binding affinity with TNF-α and IL-1β. The functionalization of boron nitride (B12N12/B16N16) nanoclusters with glycine in gaseous and aqueous environments were studied. The corresponding changes of spectroscopic, electronic, and thermodynamic properties of the B12N12 and B16N16 nanoclusters were evaluated by means of the density functional theory (DFT) calculations. Analysis of the binding energies shows that the interaction of glycine amino acid toward B12N12 is more remarkable than B16N16 in the gas and solvent environments. Thermodynamic properties also indicate that the glycine molecule energetically prefers to interact with the B12N12 and B16N16 nanoclusters through its amine group rather than carbonyl and hydroxyl groups. Our calculations also demonstrated that the electronic features of B12N12 and B16N16 nanoclusters on the adsorption of glycine from its carbonyl group in the aqueous environment is more altered than the amine and hydroxyl groups. Molecular docking shows that the [(NH2)-Glycine]2/B12N12 complex has a good binding affinity with protein tumor necrosis factor-alpha (TNF-α) and interleukin-1β (IL-1β) in comparison with the other glycine-BN nanocluster complexes thus making this hybrid bio-inorganic medium a promising material for biomedical and drug-delivery applications.