Abstract
The interaction between colloidal TiO 2 and human serum albumin (HSA) was studied by using absorption, fluorescence and synchronous fluorescence spectroscopic measurements. Colloidal TiO 2 effectively quenched the intrinsic fluorescence of HSA. The number of binding sites ( n) and apparent binding constant ( K) were calculated by fluorescence quenching data. The interaction between colloidal TiO 2 and HSA occurs through static quenching and conformational changes of HSA were observed.
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