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荧光光谱法研究塞曲司特与牛血清白蛋白的相互作用
引用本文:浦迎秋,陶伟博. 荧光光谱法研究塞曲司特与牛血清白蛋白的相互作用[J]. 药学与临床研究, 2007, 15(4): 287-291
作者姓名:浦迎秋  陶伟博
作者单位:南京市口腔医院,南京,210008;江苏省药物研究所,南京,210009
摘    要:目的:研究不同pH条件下塞曲司特与牛血清白蛋白的相互作用机制.方法:利用荧光光谱法,并以Stern-Volmer方程确定药物与蛋白的作用类型.结果:根据Stern-Volmer方程求出了不同二者pH条件下塞曲司特与牛血清白蛋白之间的猝灭常数,并依据 Foster能量转移理论确定了生理条件下药物与蛋白的结合距离为 2.53 nm.结论:在pH 5.0和人体生理pH条件下塞曲司特对牛血清白蛋白具有荧光猝灭作用且为动态猝灭过程,在pH 8.4时塞曲司特与牛血清白蛋白之间的猝灭为静态猝灭;人体生理pH条件下塞曲司特与牛血清白蛋白之间相互作用力主要为范德华力.

关 键 词:塞曲司特  牛血清蛋白  荧光光谱法  结合距离  猝灭机理
文章编号:1673-7806(2007)04-287-05
收稿时间:2007-01-12
修稿时间:2007-01-12

Studies on the interaction between seratrodast and bovine serum albumin by fluorescence spectroscopy
PU Ying-qiu and TAO Wei-bo. Studies on the interaction between seratrodast and bovine serum albumin by fluorescence spectroscopy[J]. Pharmacertical and Clinical Research, 2007, 15(4): 287-291
Authors:PU Ying-qiu and TAO Wei-bo
Affiliation:1 Stomatology Hospital of Nanjing, Nanjing 210008, China; 2 Jiangsu Provmctal Institute of Materia Medica, Nanjing 210009, China
Abstract:Objective:To study the interaction between seratrodast and bovine serum albumin (BSA) at different pH. Method: Using fluorescence spectroscopy and based on the equation of Stern-Volmer, we have determined the interaction type between drug and BSA. Results: The quenching constant was calculated according to the equation of Stern-Volmer. And according to the Foster dipole-dipole energy transfer there come to the distance between seratrodast and BSA of 2.53 nm. Conclusions: It was proved that the interaction between seratrodast and BSA is dynamic quenching in physiological solution and at pH=5.0. The interaction between seratrodast and BSA is static quenching at pH 8.4. And the Vander waals forces plays major role in the binding reaction in physiological solution.
Keywords:Seratrodast    Bovine serum albumin    Fluorescence spectroscopy    Binding distance    Quenching mechanism
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