US EPA

1492559 

Journal Article 

Study on the interaction between ICT fluorescence probe and bovine serum albumins 

Liu, YF; Li, JQ; Xu, ZC; Wei, YL; Shuang, SM; Dong, C 

2008 

Yes 

Guangpuxue yu Guangpu Fenxi / Spectroscopy and Spectral Analysis
ISSN: 1000-0593 

28 

4 

887-890 

English 

WOS:000255492300040 

The present article studied the interaction between intramolecular charge transfer fluorescence probe-1-keto-2-(p-dimethylaminobenzal)-tetrohydronaphthalene (KDTN) and bovine serum albumins (BSA). With the concentration of KDTN increasing, the fluorescence of BSA rapidly quenched and the fluorescence peak gradually blue-shifted. The result indicated that they were bound mainly by hydrophobic interaction. The binding sites is 0.94 (3 degrees C) and the equilibrium constant K is 3.27 x 10(4) L . mol(-1). Temperature increment is advantageous to the combination. It is a single static quenching process that the fluorescence of BSA quenches, which is induced by the combination of KDTN and BSA. Further study showed that different substances had different effects on the combination of KDTN and BSA. 

1-keto-2-(p-dimethylaminobenzal)-tetrohydro naphthalene; bovine serum albumin; fluorescence quenching; hydrophobic interaction