http://jcps.bjmu.edu.cn

中国药学(英文版) ›› 2016, Vol. 25 ›› Issue (3): 196-200.DOI: 10.5246/jcps.2016.03.023

• 【研究论文】 • 上一篇    下一篇

荧光光谱法研究异甘草素与牛血清白蛋白之间的相互作用

韩博1, 龙飞1, 于玮1, 陈文1*, 王新春1, 郭刚2, 周良学2   

  1. 1. 石河子大学 药学院, 新疆 石河子 832002
    2. 四川大学 生物治疗国家重点实验室, 四川 成都 610041
  • 收稿日期:2015-10-29 修回日期:2015-11-27 出版日期:2016-03-29 发布日期:2015-12-15
  • 通讯作者: Tel.: 0993-2057010, E-mail: chen-wen2000@126.com
  • 基金资助:

    National Natural Science Foundation of China (Grant No. 81560699), Scientific and Technological Project of the Science and Technology Department of Guangdong Province (Grant No. 2014A020209026), Social Development Research and Technology Transfer Program (Grant No. 2015AD002), Outstanding Young Scientific Personnel Training Plan of Shihezi University (Grant No. 2015-ZRKXJQ08).

Interaction of isoliquiritigenin with bovine serum albumin studied by fluorescence quenching method

Bo Han1, Fei Long1, Wei Yu1, Wen Chen1*, Xinchun Wang1, Gang Guo2, Liangxue Zhou2   

  1. 1. School of Pharmacy, Shihezi University, Shihezi 832002, China
    2. State Key Laboratory of Biotherapy and Cancer Center, and Department of Neurosurgery, West China Hospital, West China Medical School, Sichuan University, Chengdu 610041, China
  • Received:2015-10-29 Revised:2015-11-27 Online:2016-03-29 Published:2015-12-15
  • Contact: Tel.: 0993-2057010, E-mail: chen-wen2000@126.com
  • Supported by:
    National Natural Science Foundation of China (Grant No. 81560699), Scientific and Technological Project of the Science and Technology Department of Guangdong Province (Grant No. 2014A020209026), Social Development Research and Technology Transfer Program (Grant No. 2015AD002), Outstanding Young Scientific Personnel Training Plan of Shihezi University (Grant No. 2015-ZRKXJQ08).

摘要:

甘草素是传统中药甘草中的重要活性成分之一,本工作的目的是明确异甘草素与牛血清蛋白之间的相互作用。我们讨论了异甘草素导致牛血清蛋白荧光淬灭的机制, 通过荧光淬灭法测定了结合位点数n表观结合常数K, 计算了不同温度下的热力学常数ΔH0, ΔG0, ΔS0。通过Förster理论计算了异甘草素和牛血清蛋白之间的结合距离r, 同步荧光光谱和紫外可见吸收光谱表明牛血清蛋白的结构发生了改变。

关键词: 异甘草素, 牛血清蛋白, 热力学常数, 能量传递

Abstract:

Interaction of ioliquiritigenin (ISL), which is the main active component of a commonly used traditional Chinese medicine (TCM) Glycyrrhiza uralensis Fisch. with bovine serum albumin (BSA) has been investigated. The quenching mechanism of fluorescence of bovine serum albumin by ISL was discussed. The binding sites number n and apparent binding constant K were measured by fluorescence quenching method. The thermodynamic parameters ΔH0, ΔG0, ΔS0 at different temperatures were calculated. The distance r between donor (bovine serum albumin) and acceptor (ISL) was obtained according to Förster theory of non-radiation energy transfer. The results of synchronous fluorescence spectra and UV-vis absorption spectra show that the conformation of bovine serum albumin has been changed.

Key words: Isoliquiritigenin, Bovine serum albumin, Thermodynamic parameters, Energy transfer

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