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.

锑（Sb）的毒性与其化学形态密切相关。为进一步了解不同形式锑的毒性风险，采用多光谱方法研究了酒石酸锑钾/焦锑酸钾与牛血清白蛋白（BSA）的单独和同时结合机制。荧光猝灭结果和紫外-可见吸收光谱表明，酒石酸锑钾/焦锑酸钾与 BSA 通过适度的结合力形成了 1:1 的复合物。结果表明，酒石酸锑钾/焦锑酸钾与BSA的结合引起BSA二级结构的改变。两种 Sb 形式（酒石酸锑钾和焦锑酸钾）在共存时都能够与 BSA 相互作用，但对它们与 BSA 的相互作用存在结合影响。