畜牧与饲料科学 ›› 2015, Vol. 36 ›› Issue (8): 19-19.doi: 10.12160/j.issn.1672-5190.2015.08.006

• 基础科学 • 上一篇    下一篇

基于分子对接技术模拟预测黄连用于清热解毒物质基础

陈淑妍 程诗琦 马世堂   

  1. 安徽科技学院食品药品学院,安徽凤阳233100
  • 出版日期:2015-08-20 发布日期:2015-08-20
  • 通讯作者: 陈淑妍
  • 作者简介:作者简介:陈淑妍(1990-),女,所学专业为中药复杂成分药效物质基础。
  • 基金资助:
    项目来源:国家级大学生创新创业计划项目(201310879009).

Simulation and Prediction of Material Foundation of Coptis chinensis Franch. for Clearing Away Heat and Toxic Material Based on Molecular Docking Technology

CHEN Shu-yan, CHENG Shi-qi, MA Shi-tang (Food and Drug College,Anhui Science and Technology University, Fengyang 233100, China)   

  • Online:2015-08-20 Published:2015-08-20

摘要: [目的]采用分子对接技术模拟预测黄连用于清热解毒物质基础。[方法]建立黄连活性成分数据库,采用薛定谔Maestro8.5软件,以清热解毒蛋白LTA4H抑制剂KEL作为配体.建立LTA4H的活性位点,对黄连中活性成分进行分子对接模拟预测。[结果]以自带配体kelatorphan(-4.071)为阈值,黄连中共有14种成分与LTA4H分子对接DockingScore在阈值之上。黄连中活性成分主要作用于以Lys565、Gly268、Gly269、Arg563、Tyr378、Tyr267等氨基酸残基组成的活性位点。 [结论]黄连中活性成分与LTA4H能够成功进行分子对接,其对接位点信息有助于该类化合物清热解毒活性机制的阐释。

Abstract: [ Objective ] To apply molecular docking technology to virtually screen the active molecules, and to explore the effective substances of Coptis chinensis Franch. and the target of leukotriene A4 hydrolase (LTA4H). [ Methods ] The database of active components of Coptis ehirtensis Franch. was established by using Schrodinger Maestro 8.5 software, and the active site of LTA4H was established by using the inhibitor KEL against protein LTA4H as ligands. Molecular docking was performed to screen the active components in Coptis ehinensis Franeh.. [Results] When the Coptis chirtensis Franch. built-in ligand kelatorphan (-4.071) was set as the threshold, the Docking Score of molecular docking of fourteen kinds of component with LTA4H were above the threshold. Various active components of Coptis chinensis Franch. can function in the active site of Lys565, Gly268, Gly269, Arg563, Tyr378 and Tyr267 amino acid residues. [Conclusions]Active components in Coptis chinensis Franch. and LTA4H could successfully achieve the molecular docking. The docking site information might be helpful for the understanding of mechanism underlying the compounds inhibit LTA4H.

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