物理化学学报 >> 2005, Vol. 21 >> Issue (07): 792-795.doi: 10.3866/PKU.WHXB20050718

研究简报 上一篇    下一篇

头孢地嗪钠与牛血清白蛋白相互作用研究

邵爽; 马博英; 王学杰; 张佳捷; 李雪锋; 秦青   

  1. 浙江教育学院化学系, 杭州 310012；河北药物研究所, 石家庄 050061
  • 收稿日期:2004-12-07 修回日期:2005-02-28 发布日期:2005-07-15
  • 通讯作者: 邵爽 E-mail:sshao@zjei.net

Study on the Interaction between Cefodizime Sodium and Bovine Serum Albumin

SHAO Shuang; MA Bo-ying; WANG Xue-jie; ZHANG Jia-jie; LI Xue-feng; QIN Qing   

  1. Department of Chemistry, Zhejiang Education Institute, Hangzhou 310012； Matieria Medical Insitute of Hebei Province, Shijiazhuang 050061
  • Received:2004-12-07 Revised:2005-02-28 Published:2005-07-15
  • Contact: SHAO Shuang E-mail:sshao@zjei.net

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摘要： 用荧光光谱法研究水溶液中头孢地嗪钠(CDZM)与牛血清白蛋白(BSA)的结合反应, 测定了头孢地嗪钠与牛血清白蛋白的结合常数和结合位点数, 探讨了其荧光猝灭机制. 根据热力学参数确定了头孢地嗪钠与牛血清白蛋白之间的作用力类型, 运用Föster偶极-偶极非辐射能量转移原理, 测定了头孢地嗪钠与牛血清白蛋白相互结合时其授体-受体间的距离, 采用同步荧光技术考察了头孢地嗪钠对牛血清白蛋白构象的影响.

关键词: 头孢地嗪钠, 牛血清白蛋白, 荧光猝灭

Abstract: The binding reaction between cefodizime sodium (CDZM) and bovine serum albumin (BSA) in aqueous solution was studied by fluorescence spectra. The binding constant KA was found to be 5.31×104 and the binding sits n to be 0.94 at 299 K by fluorescence quenching method. The quenching mechanism of fluorescence of BSA by cefodizime sodium has been discussed. The thermodynamic parameters of binding reaction were determined as follows： the molar change of enthalpy ΔrHm=－15.8 kJ•mol-1, the molar change of Gibbs function ΔrGm=－27.0 kJ•mol-1 and the molar change of entropy ΔrSm=－90.0 J•K-1•mol-1, and the binding power between cefodizime sodium and bovine serum albumin has been considered. Furthermore, the binding distance (r=3.13 nm) between cefodizime sodium and bovine serum albumin was obtained according to the theory of Föster′s dipile-dipile non-radiation energy transfer mechanism, and the effect of cefodizime sodium on the conformation of bovine serum albumin was analyzed using synchronous fluorescence spectrometry.

Key words: Cefodizime sodium, Bovine serum albumin, Fluorescence quenching