Abstract
The interactions of bovine serum albumin (BSA) with phosphotungstic heteropoly acid (PW), silicon tungsten heteropoly acid (SiW) and silicon tungsten-cobalt acid (SiWCo) were studied by fluorescence spectroscopy and UV absorption spectroscopy at Tris buffer solution (pH = 7.40). It was found that the fluorescence quenching of PW, SiW and SiWCo with BSA was static and the binding constant, binding site and the thermodynamic parameters were calculated at 298 and 310K. In addition, the conformations of BSA impacted by PW, SiW and SiWCo were researched using synchronous fluorescence. The results showed that PW, SiW and SiWCo all could interact with BSA but they had not changed the conformation of BSA.
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