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

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-alpha) and interleukin-1 beta (IL-1 beta) 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. (C) 2021 Elsevier B.V. All rights reserved.

Automated summary

The functionalization of boron nitride nanoclusters with glycine in gaseous and aqueous environments was studied using density functional theory calculations. The results showed that glycine has a more remarkable interaction with B12N12 compared to B16N16, and energetically prefers to interact with nanoclusters through its amine group. The electronic features of nanoclusters on the adsorption of glycine from its carbonyl group in the aqueous environment are more altered than the amine and hydroxyl groups. Additionally, molecular docking demonstrated the potential of the glycine-B12N12 complex for biomedical and drug-delivery applications.