Difference in the binding mechanism of distinct antimony forms in bovine serum albumin.

The toxicity of antimony (Sb) is closely related to its chemical forms. To further realize the toxicity risk of different forms of Sb, the separate and simultaneous binding mechanisms of antimony potassium tartrate/potassium pyroantimonate with bovine serum albumin (BSA) were investigated with muti-spectroscopic methods. Fluorescence quenching result and UV-vis absorption spectra showed that a 1:1 complex was formed between antimony potassium tartrate/potassium pyroantimonate and BSA through a modest binding force. The results revealed that the binding of antimony potassium tartrate/potassium pyroantimonate to BSA caused changes in the secondary structure of BSA. Both Sb forms (antimony potassium tartrate and potassium pyroantimonate) were able to interact with BSA when coexisting but there was a binding influence on their interacting with the BSA. Both Sb forms interfere with the binding of the other to protein.