Open AccessThe fluorescence spectroscopic study on the interaction between 3-ethyl-benzothiazospironaphthopyran and bovine serum albumin
Author(s) -
Jie Liu,
Jianghua Liu
Publication year - 2021
Publication title -
iop conference series. earth and environmental science
Language(s) - English
Resource type - Journals
eISSN - 1755-1307
pISSN - 1755-1315
DOI - 10.1088/1755-1315/772/1/012045
Subject(s) - bovine serum albumin , fluorescence , ionic strength , chemistry , titration , quenching (fluorescence) , fluorescence spectroscopy , analytical chemistry (journal) , molecule , ionic bonding , spectroscopy , chromatography , ion , organic chemistry , aqueous solution , physics , quantum mechanics
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 7.91×10 4 L mol -1 , 6.60×10 4 L mol -1 , and 5.22×10 4 L mol -1 . The values of the latter is 0.88, 0.98, and 1.00.