Docking study on the binding property of Metronidazole to Human serum albumin

Human serum albumin (HSA) is one of the main endogenous vehicles for biodistribution of molecules by blood plasma. Association constants and thermodynamic parameters for the interaction of HSA with Metronidazole were studied by docking. Docking study suggests that Metronidazole is able to interact with HSA by means of hydrogen bonds two lysine , two arginine residues, whereas the N-O group is inserted in a hydrophobic pocket, close to Trp-214. The Estimated of Gibbs free energies( ΔG° (kcal/mol)) is equal to -4.98 for the best model. The negative values of ΔG° indicate a spontaneous process. The association constant value (Ka ≈ 3.97×103 L·mol−1) is favorable for its efficient biodistribution by blood plasma.

Keywords:

Human serum albumin , Metronidazole , Docking , Thermodynamic parameters