Antioxidant activity, β-LG and HSA interactions of a novel tetradentate Schiff base Pd(II) complex

The drug-protein interaction also has a prevailing contribution to drug temperament and effectiveness as the bound fraction of drug is a depository while the free fraction of drug exhibits pharmacological properties. therefore, It is essential to investigate the interactions between drugs and a carrier protein in order to specify the pharmacology andpharmacodynamics of drugs (1, 2). Pd(II) Schiff base complex by 3,4-diaminobenzophenone and diacetyl monoxime was synthesized. This complex was characterized by FT-IR, 1H NMR, UV–Vis spectroscopies and molar conductance. This complex was studied for in vitro antioxidant activity as radical scavengers. Antioxidant activity of Pd complex was obtained IC50 = 55 mg L-1. Protein interaction (Human serum albumin, HSA, and β-lactoglobulin, β-LG) were done. Our results show that this complex quenched the fluorescence of both protein by static mechanism and Pd complex with HSA showed a stronger binding ability than that of β- LG. Thermodynamic studies showed that Hydrogen bonds and Van der Waals forces in both examined systems were the main stabilizing forces in the development of drug-protein complex.