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化学学报
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化学学报 ›› 2005, Vol. 63 ›› Issue (23): 2169-2173. 上一篇    下一篇

研究论文

几种抗生素与人血清白蛋白结合反应的研究

毕淑云1,2, 丁兰1, 宋大千1, 田媛1, 张寒琦1   

  1. 1. 吉林大学化学学院, 长春, 130012;
    2. 延边大学理工学院化学系, 延吉, 133002
  • 投稿日期:2005-02-18 修回日期:2005-05-08 发布日期:2014-02-14
  • 通讯作者: analchem@mail.jlu.edu.cn
  • 作者简介:张寒琦,E-mail:analchem@mail.jlu.edu.cn
  • 基金资助:

    吉林省科技发展计划项目(No.20040561);高等学校博士学科点科研基金(No.2003183035)资助课题.

Studies on the Binding Mechanism of Several Antibiotics and Human Serum Albumin

BI Shu-Yun1,2, DING Lan1, SONG Da-Qian1, TIAN Yuan1, ZHANG Han-Qi1   

  1. 1. College of Chemistry, Jilin University, Changchun 130012;
    2. Chemistry Department, College of Science and Engineering, Yanbian University, Yanji 133002
  • Received:2005-02-18 Revised:2005-05-08 Published:2014-02-14

PDF

1476

被引次数

92

用荧光法研究了头孢噻肟钠、苯唑西林、阿莫西林、诺氟沙星、依诺沙星等五种抗生素类药物与人血清白蛋白的结合反应,测得26℃时的结合常数KA分别为1.98×104,1.01×103,1.38×103,5.97×104和7.15×104L·mol-1,结合位点数n分别为1.16,0.86,1.19,0.91和0.93.确定了这些药物与人血清白蛋白之间的主要结合力为静电作用力.

关键词: 人血清白蛋白, 头孢噻肟钠, 苯唑西林, 阿莫西林, 诺氟沙星, 依诺沙星, 荧光光谱法

The binding characteristics of antibiotics, cefotaxime sodium, oxacillin, amoxicillin, norfloxacin and enoxacin with human serum albumin (HSA) were studied by fluorescence spectrometry. These drugs quenched the HSA fluorescence via a nonradiative energy transfer mechanism. The binding constants (KA) and binding sites (n) for drug-HSA were obtained by an improved analysis method to process the experi-mental data. The values of KA obtained were 1.98×104, 1.01×103, 1.38×103, 5.97×104 and 7.15×104 L·mol-1 for cefotaxime sodium-HSA, oxacillin-HSA, amoxicillin-HSA, norfloxacin-HSA and enox-acin-HSA, respectively, at 26℃. The values of n were 1.16, 0.86, 1.19, 0.91 and 0.93, respectively, for these drugs in the above order. The electrostatic interaction was found to be main acting force in the studied systems.

Key words: human serum albumin, cefotaxime sodium, oxacillin, amoxicillin, norfloxacin, enoxacin, fluo-rescence quenching