高等学校化学学报 ›› 2014, Vol. 35 ›› Issue (2): 309-313.doi: 10.7503/cjcu20130748

• 有机化学 • 上一篇    下一篇

青蒿截疟组合物与牛血清白蛋白的相互作用

王满元(), 张超, 李静, 李朝霞, 龚慕辛()   

  1. 首都医科大学中医药学院, 北京 100069
  • 收稿日期:2013-08-03 出版日期:2014-02-10 发布日期:2013-12-26
  • 作者简介:联系人简介: 王满元, 男, 博士, 副教授, 主要从事中药活性成分及炮制原理研究. E-mail:wangmyjun@aliyun.com; 龚慕辛, 女, 博士, 教授, 博士生导师, 主要从事中药制剂研究. E-mail:gongmuxin@126.com
  • 基金资助:
    国家自然科学基金(批准号: 81102752)、 北京市自然科学基金(批准号: 2112010)和北京市属高等学校高层次人才引进与培养计划项目(批准号: CIT&TCD201304184)资助

Interaction of Antimalarial Components Combination from Artemisia annua L. with Bovine Serum Albumin

WANG Manyuan*(), ZHANG Chao, LI Jing, LI Zhaoxia, GONG Muxin*()   

  1. School of Traditional Chinese Medicine, Capital Medical University, Beijing 100069, China
  • Received:2013-08-03 Online:2014-02-10 Published:2013-12-26
  • Contact: WANG Manyuan,GONG Muxin E-mail:wangmyjun@aliyun.com;gongmuxin@126.com
  • Supported by:
    † Supported by the National Natural Science Foundation of China(No.81102752), Beijing Natural Science Foundation, China(No.2112010) and Funding Program for Introduction of High-level Talent and Training Program in Institutions of Higher Learning Under the Jurisdiction of Beijing, China(No.CIT&TCD201304184)

摘要:

利用荧光光谱法研究青蒿截疟组合物(青蒿素、 青蒿乙素、 青蒿酸与东莨菪内酯质量比为1∶1∶1∶1的混合体系, AAAS)与牛血清白蛋白(BSA)的相互作用. 结果表明, 与青蒿素单独作用相比, AAAS对BSA的荧光猝灭作用增强, 并以静态猝灭为主; 计算了298, 303和310 K下的结合常数、 结合位点数和热力学参数, 表明AAAS与BSA之间具有较强的静电引力, 相互作用过程是一个熵增加的自发分子间作用过程. AAAS对BSA的猝灭常数和结合常数均增大. 结果表明, AAAS显著增加了青蒿素与血清白蛋白的结合作用, 此过程可能是AAAS增加青蒿素抗疟疗效的重要体内环节.

关键词: 青蒿素, 截疟组合物, 牛血清白蛋白, 荧光光谱, 药物相互作用

Abstract:

The interaction of arteannuin, arteannuic acid and scopoletin on the binding of artemisinin with bovine serum albumin(BSA) was investgated by fluorescent spectrometry. BSA fluorescence quenching effect was strengthened after the interaction of BSA with antimalarial components combination[AAAS, m(artemisinin)∶m(arteannuin B)∶m(arteannuic acid)∶m(scopoletin)=1∶1∶1∶1] from Artemisia annua L. compared to that of BSA with artemisinin alone, and the fluorescence quenching effect was staitc quenching. The binding constant, binding point numbers and thermodynamic parameters at three temperature levels, for example, 298, 303 and 310 K were calculated, and the results revealed that the binding of AAAS with BSA had strong electrostatic attraction and the process was a spontaneous molecular interaction procedure in which entropy was increased. Compared with artemisinin, the quenching constants and the binding constant of AAAS with BSA were also increased. These results confirmed that arteannuin, arteannuic acid and scopoletin could significantly increased the binding of artemisinin with BSA, and the interaction of AAAS with BSA might be a key factor that improved the antimalarial efficacy of artemisinin in vivo.

Key words: Artemisinin, Antimalarial components combination, Bovine serum albumin, Fluorescence spectrum, Drug interaction

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