Complexation of HSA with different forms of antimony (Sb): An application of fluorescence spectroscopy

Antimony (Sb) pollution has been of a great environmental concern in some areas in China. Sb enters human body via drinking water, inhalation and food chain, unavoidably interacts with human serum albumin (HSA) in blood plasma, and consequently does harm to human health. The harmful effects of Sb on human health depend on the Sb species and their binding ability to HSA. In the present study, binding of three forms of Sb with HSA was investigated by excitation-emission matrix (EEM) spectroscopy. All of antimony potassium tartrate, antimony trichloride and potassium pyroantimonate quenched fluorescence of HSA. Values of conditional stability constant K_a (×10⁵/M) for Sb and HSA systems were 8.13-9.12 for antimony potassium tartrate, 2.51-4.27 for antimony trichloride and 3.63-9.77 for potassium pyroantimonate. The binding constant K_b (×10 ⁴/M) values of HSA with antimony potassium tartrate, antimony trichloride and potassium pyroantimonate were 0.02-0.07, 3.55-5.01, and 0.07-1.08, respectively. There was one independent class of binding site for antimony trichloride towards HSA. There was more than one Sb binding site and negative cooperativity between multiple binding sites for potassium pyroantimonate and antimony potassium tartrate towards HSA. The binding ability of HSA to complex Sb followed the order: antimony trichloride>potassium pyroantimonate>antimony potassium tartrate. © 2012 Elsevier B.V. All rights reserved.