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Updated: May 29, 2026
Luminophore Formation in Various Conformations of Bovine Serum Albumin by Binding of Gold(III)
Published on: August 31, 2018
The fluorescence spectroscopic study on the interaction between imidazo[2,1-b]thiazole analogues and bovine serum
Xianyong Yu1, Ying Yang, Lu Shiyu
1Key Laboratory of Theoretical Chemistry and Molecular Simulation of Ministry of Education, School of Chemistry and Chemical Engineering, Hunan University of Science and Technology, Xiangtan, China.
Abstract:
The interaction between imidazo[2,1-b]thiazole (IMTZ) and bovine serum albumin (BSA) was analyzed by fluorescence and ultraviolet spectroscopy at 302 and 310 K under simulative physiological conditions. The results show that IMTZ can effectively quench the intrinsic fluorescence of BSA via static and dynamic quenching. The binding constant, binding sites of IMTZ with BSA were calculated. According to the Förster non-radiation energy transfer theory, the average binding distance between IMTZ and BSA was obtained. What's more, the synchronous fluorescence spectra indicated that the conformation of BSA has been changed. The results provided the information for the binding of IMTZ to BSA, and the influences of substituent group on the interaction were also discussed.
