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

摘要: 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 found that intrinsic fluorescence HSA quenched by addition ] quenching mechanism considered as static formation ]-HSA complex. The binding constant about 104  M-1 at room temperature. values calculated thermodynamic parameters (ΔH   0) suggested both hydrogen bonds hydrophobic interactions were involved process. site marker competitive experiments revealed to primarily occurred subdomain IIIA (site II) HSA. results circular dichroism (CD) UV-vis spectroscopy showed micro-environment amino acid residues conformation changed after Finally, modelled molecular docking method. Excellent agreement obtained experimental theoretical with respect forces constant.