| Studies on Thermodynamics Features of the Interaction between Imidacloprid and Bovine Serum Albumin |
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| 引用本文： | 颜承农 梅平 关中杰 刘义. Studies on Thermodynamics Features of the Interaction between Imidacloprid and Bovine Serum Albumin[J]. 中国化学, 2007, 25(8): 1085-1089. DOI: 10.1002/cjoc.200790202 |
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| 作者姓名： | 颜承农 梅平 关中杰 刘义 |
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| 作者单位： | [1]College of Chemistry and Environmental Engineering, Yangtze University, Jingzhou, Hubei 434023, China [2]College of Chemistry and Molecular Sciences, Wuhan University, Wuhan, Hubei 430072, China |
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| 基金项目： | Project supported by the National Natural Science Foundation of China （Nos. 30570015, 20373051） and Natural Science Foundation of Hubei Province of China （Nos. 2005ABA067, 2005ABC002）. |
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| 摘 要： | At different temperatures, the interactions between imidacloprid （IMI） and bovine serum albumin （BSA） were investigated with a fluorescence quenching spectrum, a synchronous fluorescence spectrum, a three-dimensional fluorescence spectrum and an ultraviolet-visible spectrum. The average values of bonding constants （KLB： 3.424 × 10^4 L,mol^-1）, thermodynamic parameters （△H： 5.188 kJ,mol^-1, △G^（○—）：-26.36 kJ,mol^-1, △S： 103.9 J,K^-1,mol^-1） and the numbers of bonding sites （n： 1.156） could be obtained through Stern-Volmer, Lineweaver-Burk and ther- modynamic equations. It was shown that the fluorescence of BSA could be quenched for its reactions with IMI to form a certain kind of new compound. The quenching belonged to a static fluorescence quenching, with a non-radiation energy transfer happening within a single molecule. The thermodynamic parameters agree with △H〉 0, △S〉0 and△G^（○-）〈0, suggesting that the binding power between IMI and BSA should be mainly a hydrophobic interaction.
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| 关 键 词： | 牛血清白蛋白 荧光光谱 三维荧光 热力学 |
| 修稿时间： | 2006-10-302007-04-20 |
Studies on Thermodynamics Features of the Interaction between Imidacloprid and Bovine Serum Albumin |
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| YAN Cheng-Nong,MEI Ping,GUAN, Zhong-Jie,LIU Yi. Studies on Thermodynamics Features of the Interaction between Imidacloprid and Bovine Serum Albumin[J]. Chinese Journal of Chemistry, 2007, 25(8): 1085-1089. DOI: 10.1002/cjoc.200790202 |
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| Authors: | YAN Cheng-Nong MEI Ping GUAN Zhong-Jie LIU Yi |
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| Affiliation: | 1.College of Chemistry and Environmental Engineering, Yangtze University, Jingzhou, Hubei 434023, China ;2.College of Chemistry and Molecular Sciences, Wuhan University, Wuhan, Hubei 430072, China |
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| Abstract: | At different temperatures, the interactions between imidacloprid (IMI) and bovine serum albumin (BSA) were investigated with a fluorescence quenching spectrum, a synchronous fluorescence spectrum, a three‐dimensional fluorescence spectrum and an ultraviolet‐visible spectrum. The average values of bonding constants (KLB: 3.424×104 L·mol?1), thermodynamic parameters (ΔH: 5.188 kJ·mol?1, ΔG(:?26.36 kJ·mol?1, ΔS: 103.9 J·K?1·mol?1) and the numbers of bonding sites (n: 1.156) could be obtained through Stern‐Volmer, Lineweaver‐Burk and thermodynamic equations. It was shown that the fluorescence of BSA could be quenched for its reactions with IMI to form a certain kind of new compound. The quenching belonged to a static fluorescence quenching, with a non‐radiation energy transfer happening within a single molecule. The thermodynamic parameters agree with ΔH>0, ΔS>0 and ΔGσ<0, suggesting that the binding power between IMI and BSA should be mainly a hydrophobic interaction. |
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| Keywords: | imidacloprid bovine serum albumin fluorescence spectrum three-dimensional fluorescence spectrum thermodynamic parameter |
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