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›› 2009, Vol. 9 ›› Issue (1): 118-122.

• 生化工程专栏 • 上一篇    下一篇

荧光光谱法研究紫草素与牛血清白蛋白的相互作用

葛锋 王剑平 刘迪秋 陈朝银 韩本勇 王玉春   

  1. 昆明理工大学生命科学与技术学院 昆明理工大学生命科学与技术学院 昆明理工大学生命科学与技术学院 昆明理工大学生命科学与技术学院 昆明理工大学生命科学与技术学院 中国科学院过程工程研究所生化工程国家重点实验室 北京100080
  • 收稿日期:2008-07-04 修回日期:2008-11-18 出版日期:2009-02-20 发布日期:2009-02-20
  • 通讯作者: 葛锋

Study on Interaction between Shikonin and Bovine Serum Albumin by Fluorescence Spectra

GE Feng WANG Jian-feng LIUDi-qiu CHEN Chao-yin HAN Ben-yong WANG Yu-chun   

  1. College of Life Science and Technology, Kunming University of Science and Technolog College of Life Science and Technology, Kunming University of Science and Technolog College of Life Science and Technology, Kunming University of Science and Technolog College of Life Science and Technology, Kunming University of Science and Technolog College of Life Science and Technology, Kunming University of Science and Technolog Inst. Process Eng., Chinese Academy of Sciences
  • Received:2008-07-04 Revised:2008-11-18 Online:2009-02-20 Published:2009-02-20
  • Contact: GE Feng

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被引次数

24

摘要： 采用荧光光谱法研究了紫草素和牛血清白蛋白的相互作用. 实验结果表明，紫草素对牛血清白蛋白的荧光有明显的猝灭作用，其方式为静态猝灭，紫草素与牛血清白蛋白之间发生了分子内非辐射能量转移；紫草素和牛血清白蛋白的结合位点数为1，结合位置距离212位色氨酸残基1.92 nm；温度为22和36℃时，紫草素对牛血清白蛋白荧光的猝灭常数分别为6.96′104和5.91′104 mol/L. 热力学分析表明，紫草素与蛋白之间的结合以静电作用力为主. 同时，紫草素分子含有多个羟基，它们之间还存在氢键作用力.

关键词: 紫草素, 牛血清白蛋白, 荧光光谱, 相互作用

Abstract: The interaction between shikonin and bovine serum albumin (BSA) was studied by fluorescence spectra. The results showed that shikonin strongly quenched the fluorescence of bovine serum albumin. The quenching mechanism was a static quenching procedure, and non-radiation energy transfer happened among molecules. The number of binding site was 1, and the binding locality was a distance of 1.92 nm away from tryptophan residue-212 in BSA. At 22 and 36℃, the quenching constant of BSA and shikonin system was 6.96×104 and 5.91×104 mol/L. Thermodynamic analysis showed that binding power between shikonin and BSA was electrostatic interaction mainly. In addition, several hydroxyl groups were in the molecular structure of shikonin, therefore, there was also hydrogenolysis interaction between shikonin and BSA.

Key words: shikonin, bovine serum albumin, fluorescence spectra, interaction

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