Interaction studies of copper complex containing food additive carmoisine dye with human serum albumin (HSA): Spectroscopic investigations.

Abstract

In this study, the interaction between human serum albumin (HSA) and a copper complex of carmoisine dye; [Cu(carmoisine)2 (H2 O)2 ], was studied in vitro using multi-spectroscopic methods. It was found that the intrinsic fluorescence of HSA was quenched by the addition of the [Cu(carmoisine)2 (H2 O)2 ] complex and the quenching mechanism was considered as static quenching by formation of a [Cu(carmoisine)2 (H2 O)2 ]-HSA complex. The binding constant was about 104 M-1 at room temperature. The values of the calculated thermodynamic parameters (ΔH<0 and ΔS>0) suggested that both hydrogen bonds and the hydrophobic interactions were involved in the binding process. The site marker competitive experiments revealed that the binding of [Cu(carmoisine)2 (H2 O)2 ] to HSA primarily occurred in subdomain IIIA (site II) of HSA. The results of circular dichroism (CD) and UV-vis spectroscopy showed that the micro-environment of amino acid residues and the conformation of HSA were changed after addition of the [Cu(carmoisine)2 (H2 O)2 ] complex. Finally, the binding of the [Cu(carmoisine)2 (H2 O)2 ] complex to HSA was modelled by a molecular docking method. Excellent agreement was obtained between the experimental and theoretical results with respect to the binding forces and binding constant.