Molecular Docking Study of the Interactions between Nalidixic acid with Human Serum Albumin

Human serum albumin (HSA) is one of the main endogenous carriers for biodistribution of molecules byblood plasma. Inhabitation constants and thermodynamic parameters (ΔH and ΔG) for the interaction ofHSA with nalidixic acid were studied by molecular docking. The hydrogen-bond forces were found tostabilize the nalidixic acid–HSA complex. Furthermore, the molecular modeling was employed forcharacterization of drug binding sites and interaction of nalidixic acid with amino acid residues. Resultsconfirmed the presence of this drug in 1 site of HSA and indicated that the driving force between NA andHSA was mainly typical hydrophilic interaction.

Keywords:

Molecular Docking , Interaction , Nalidixic acid , HAS