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

Hamed Khorami¹ Mahdi Moosazadeh² Matin Khorami³

1) Department of Medicinal Chemistry, Ghadr University Of Kochesfahan, Guilan, Iran
2) Psychology Department Islamic Azad University Of Rasht, Guilan, Iran
3) student

Publication : 4th International Congress on Engineering, Technology and Applied Science - Auckland University of Technology(etas2019.com)
Abstract :
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 Tinidazole were studied by docking. Docking study suggests that Tinidazole 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 bio distribution by blood plasma.
Keywords : Human serum albumin Tinidazole Docking Thermodynamic parameters.