The interaction between 4-（4-hydroxybut-2-ynyloxy）-3-（phenylsulfonyl）-1,2,5-oxadiazole-2-oxide （FB） and bovine serum albumin （BSA） was studied by spectroscopic methods including fluorescence and UV-Vis absorpt...The interaction between 4-（4-hydroxybut-2-ynyloxy）-3-（phenylsulfonyl）-1,2,5-oxadiazole-2-oxide （FB） and bovine serum albumin （BSA） was studied by spectroscopic methods including fluorescence and UV-Vis absorption spectroscopy. The quenching mechanism of fluorescence of BSA by FB was considered to be a dynamic quenching procedure. The number of binding sites n and apparent binding constant K were measured by fluorescence quenching method. The results indicate that there is FB molecular binding with BSA, and forming 1 ： 1 complex. The thermodynamic parameters such as △H, △G and △S, etc., were calculated, The results indicate that the binding reaction is mainly entropy-driven and hydrophobic forces play major role in the binding reaction, The distance r between donor （BSA） and acceptor （FB） was obtained according to Forster theory of non-radioactive energy transfer.展开更多
基金Project supported by the National Natural Science Foundation of China （Nos. 30570015, 20373051 ）, the Natural Science Foundation of Hubei Province （Nos. 2006ABA333, 2005ABC002）, and the Science Foundation of Hubei Provincial Educational Department （No. D200528003）, and the Science Research Foundation of Chinese Ministry of Education （No. [2006]8IRT0543）.
文摘The interaction between 4-（4-hydroxybut-2-ynyloxy）-3-（phenylsulfonyl）-1,2,5-oxadiazole-2-oxide （FB） and bovine serum albumin （BSA） was studied by spectroscopic methods including fluorescence and UV-Vis absorption spectroscopy. The quenching mechanism of fluorescence of BSA by FB was considered to be a dynamic quenching procedure. The number of binding sites n and apparent binding constant K were measured by fluorescence quenching method. The results indicate that there is FB molecular binding with BSA, and forming 1 ： 1 complex. The thermodynamic parameters such as △H, △G and △S, etc., were calculated, The results indicate that the binding reaction is mainly entropy-driven and hydrophobic forces play major role in the binding reaction, The distance r between donor （BSA） and acceptor （FB） was obtained according to Forster theory of non-radioactive energy transfer.
