College of Chemistry and Chemical Engineering, Bohai University, 19, Keji Rd., New Songshan District, Jinzhou City, Liaoning Province, 121013, People's Republic of China.
Department of Chemistry, College of Sciences, Northeastern University, Shenyang, 110819, People's Republic of China.
Biometals. 2021 Jun;34(3):493-510. doi: 10.1007/s10534-021-00291-3. Epub 2021 Feb 15.
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。为了进一步实现不同形态 Sb 的毒性风险，本研究采用多种光谱方法分别和同时研究了酒石酸氢钾/焦锑酸钾与牛血清白蛋白（BSA）的结合机制。荧光猝灭实验和紫外-可见吸收光谱表明，酒石酸氢钾/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，酒石酸氢钾/焦锑酸钾与 BSA 的结合导致 BSA 的二级结构发生变化。两种 Sb 形态（酒石酸氢钾和焦锑酸钾）在共存时都能够与 BSA 相互作用，但它们之间的相互作用存在结合影响。两种 Sb 形态都干扰了彼此与蛋白质的结合。
