Antioxidant Function and β-LG Interactions of Zinc(II) Dithiocarbamate Complex

A new dithiocarbamate complex was synthesized and characterized (Fig. 1) [1]. The in vitroantioxidant activity of Zn(II) complex was measured against 1,1-diphenyl-2-picrylhydrazylradicals (IC50 = 36 mg L-1). The interaction of the complex with bovine β-lactoglobulin (β-LG) presented that Zn(II) complex strongly quenched the fluorescence of carrier protein instatic quenching mode. Thermodynamic analysis indicated that complex binding βLG wasdriven by favorable enthalpy and unfavorable entropy, and the major driving forces were hydrogenbonding and Van der Waals forces. The results of FT-IR and UV–visible measurementsillustrated that the binding of complex to β-LG may induce conformational and microenvironmentalchanges of studied protein [2]. Molecular docking analysis confirmed thatZn(II) complex binds to residues located in the site II of β-LG.