Binding forces between bovine milk β-lactoglobulin and novel palladium(II) complex

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 β-lactoglobulin (βLG) were investigated by employing biophysical techniques at three temperatures (pH 7.4). The experimental results showed that the Pd(II) complex interacted above carrier proteins with moderate binding affinity (Kb ~̴ 0.2 × 103 M−1). Binding of Pd(II) complex to βLG caused strong fluorescence quenching of protein through static quenching mechanism. In studied system hydrogen bonds and van der Waals forces were the major stabilizing forces in the drug-protein complex formation. UV–Visible measurements indicated that the binding of above complex to βLG may induce conformational and micro-environmental changes of proteins. All these experimental results suggest that βLG might act as carrier protein for Pd(II) complex to deliver it to the target molecules.

Keywords:

β-lactoglobulin , Schiff base , Pd(II) complex , Protein interactions