Molecular Docking Study of the Interaction of Ionic liquids with HSA as Potential Antimicrobial Agents

The interaction between human serum albumin (HSA) and ionic liquids (ILs), as good potential microbial growth inhibitors, was investigated by molecular docking analysis [1]. All compounds were significant active against the tested bacterial and fungal strains [2]. The results of the molecular docking study showed that the studied ILs are able to firmly bind in the subdomain IIA of HSA. Molecular docking studies of one of ILs with the most antimicrobial activity shows the formation of a strong protein-ligand complex (Binding Energy = -6.49 kcal/mol). Two Hydrogen bonds were formed between protein and ligand. The first interaction (2.89 Å length) is formed between the Oxygen of the ligand and the NH-group of amino acid Arg218. The second interaction (2.80 Å length) is formed between NH-group of the ligand and the Oxygen of Asp451. The presence of two Hydrogen bonds in the protein-ligand system indicates the stability of this complex. Also, nine hydrophobic interactions were formed between hydrophobic substructures of the ligand and the protein. This study provides a better understanding of the binding of ILs to HSA and opens the way for their further biological and pharmaceutical investigations as candidates with antimicrobial properties.