The fluorescence spectroscopic study on the interaction between imidazo[2,1-b]thiazole analogues and bovine serum albumin.
The fluorescence spectroscopic study on the interaction between imidazo[2,1-b]thiazole analogues and bovine serum albumin.
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DOI：
10.1016/j.saa.2011.08.038
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发表时间：
2011-12
期刊：
影响因子：
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通讯作者：
Xian-yong Yu;Ying Yang;Lu Shiyu;Q. Yao;Heting Liu;Xiaofang Li;P. Yi
中科院分区：
文献类型：
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作者：
Xian-yong Yu;Ying Yang;Lu Shiyu;Q. Yao;Heting Liu;Xiaofang Li;P. Yi
在模拟生理条件下，采用荧光光谱和紫外光谱法研究了302 K和310 K下咪唑并[2，1-B]噻唑（IMTZ）与牛血清白蛋白（BSA）的相互作用。结果表明，IMTZ通过静态和动态两种方式有效地猝灭BSA的内源荧光。计算了IMTZ与BSA的结合常数、结合位点。根据Förster非辐射能量转移理论，计算了IMTZ与BSA之间的平均结合距离。同步荧光光谱表明BSA的构象发生了变化。研究结果为IMTZ与BSA的相互作用提供了理论依据，并讨论了取代基对相互作用的影响。
The interaction between imidazo[2,1-b]thiazole (IMTZ) and bovine serum albumin (BSA) was analyzed by fluorescence and ultraviolet spectroscopy at 302 and 310K 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.