Abstract
The interaction of 3-ethyl-benzothiazospironaphthopyran (BSNP) with bovine serum albumin (BSA) was analyzed by fluorescence spectroscopy. Firstly, the optimal experimental conditions, including medium, pH and ionic strength, were investigated. Secondly, the fluorescence titration experiments at 298 K, 306 K, and 313 K showed that the intrinsic fluorescence of BSA can be strongly quenched by the small organic molecule BSNP. The formation of a BSA-BSNP complex suggested that the fluorescence quenching mechanism may be a kind of static quenching procedure. Finally, the binding constants (K) and the ratio of fluorescence quantum yields of BSA-BSNP complex and free BSA (f) at three different temperatures were obtained. The values of the former were 7.91×104 L mol-1, 6.60×104 L mol-1, and 5.22×104 L mol-1. The values of the latter is 0.88, 0.98, and 1.00.
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