Binding forces between a novel Schiff base palladium(II) complex and two carrier proteins: human serum albumi and ß-lactoglobulin.

Ligand binding studies on carrier proteins are crucial in determining the pharmacological properties of drug candidates. Here, a new palladium(II) complex was synthesized and characterized. The in vitro binding studies of this complex with two carrier proteins, human serum albumin (HSA), and ß-lactoglobulin (ßLG) were investigated by employing biophysical techniques as well as computational modeling. The experimental results showed that the Pd(II) complex interacted with two carrier proteins with moderate binding affinity (Kb ≈ .5 × 104 M-1 for HSA and .2 × 103 M-1 for ßLG). Binding of Pd(II) complex to HSA and ßLG caused strong fluorescence quenching of both proteins through static quenching mechanism. In two studied systems hydrogen bonds and van der Waals forces were the major stabilizing forces in the drug-protein complex formation. UV-Visible and FT-IR measurements indicated that the binding of above complex to HSA and ßLG may induce conformational and micro-environmental changes of two proteins. Protein-ligand docking analysis confirmed that the Pd(II) complex binds to residues located in the subdomain IIA of HSA and site A of ßLG. All these experimental and computational results suggest that ßLG and HSA might act as carrier protein for Pd(II) complex to deliver it to the target molecules.