Investigations of adsorption behavior and anti-inflammatory activity of glycine functionalized Al12N12 and Al12ON11 fullerene-like cages

Abstract

The adsorption behavior of the amino acid, glycine (Gly), via the carboxyl, hydroxyl, and amino groups onto the surfaces of Al₁₂N₁₂ and Al₁₆N₁₆ fullerene-like cages were computationally evaluated by the combination of density functional theory (DFT) and molecular docking studies. It was found that Gly can chemically bond with the Al₁₂N₁₂ and Al₁₆N₁₆ fullerene-like cages as its amino group being more favorable to interact with the aluminum atoms of the adsorbents compared to carboxyl and hydroxyl groups. Oxygen and carbon doping were reported to reduce steric hindrance for Glycine interaction at Al site of Al₁₂ON₁₁/Gly and Al₁₂CN₁₁/Gly complexes. Interaction was further enhanced by oxygen doping due to its greater electron withdrawing effect. Herein, the Al₁₂ON₁₁/Gly complex where two carbonyl groups of Gly are bonded to the aluminum atoms of the Al₁₂N₁₂ fullerene-like cage is the most stable interaction configuration showing ∆_adsH and ∆_adsG values of -81.74 kcal/mol and -66.21 kcal/mol, respectively. Computational studies also revealed the frequency shifts that occurred due to the interaction process. Molecular docking analysis revealed that the Al₁₂N₁₂/Gly (-11.7 kcal/mol) and the Al₁₂ON₁₁/Gly (-9.2 kcal/mol) complexes have a good binding affinity with protein tumor necrosis factor alpha (TNF-α). TNF-α was implicated as a key cytokine in various diseases, and it has been a validated therapeutic target for the treatment of rheumatoid arthritis. These results suggest that the Al₁₂N₁₂/Gly complex in comparison with the Al₁₆N₁₆/Gly, Al₁₂ON₁₁/Gly, and the Al₁₂CN₁₁/Gly complexes could be efficient inhibitors of TNF-α.

Keywords: Adsorption; Al(12)N(12) fullerene-like cage; DFT; Glycine; Molecular docking; Tumor necrosis factor alpha.