Emodin targets the β-hydroxyacyl-acyl carrier protein dehydratase from Helicobacter pylori: enzymatic inhibition assay with crystal structural and thermodynamic characterization
文献类型：期刊论文
| 作者 | Chen,Jing2 ; Zhang,Liang2; Zhang,Yu2; Zhang,Haitao2; Du,Jiamu1; Ding,Jianping1; Guo,Yuewei2; Jiang,Hualiang2; Shen,Xu2
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| 刊名 | BMC Microbiology
 |
| 出版日期 | 2009-05-12 |
| 卷号 | 9期号:1 |
| ISSN号 | 1471-2180 |
| DOI | 10.1186/1471-2180-9-91 |
| 通讯作者 | Guo,Yuewei(ywguo@mail.shcnc.ac.cn) ; Shen,Xu(xshen@mail.shcnc.ac.cn) |
| 英文摘要 | AbstractBackgroundThe natural product Emodin demonstrates a wide range of pharmacological properties including anticancer, anti-inflammatory, antiproliferation, vasorelaxant and anti-H. pylori activities. Although its H. pylori inhibition was discovered, no acting target information against Emodin has been revealed to date.ResultsHere we reported that Emodin functioned as a competitive inhibitor against the recombinant β-hydroxyacyl-ACP dehydratase from Helicobacter pylori (HpFabZ), and strongly inhibited the growth of H. pylori strains SS1 and ATCC 43504. Surface plasmon resonance (SPR) and isothermal titration calorimetry (ITC) based assays have suggested the kinetic and thermodynamic features of Emodin/HpFabZ interaction. Additionally, to inspect the binding characters of Emodin against HpFabZ at atomic level, the crystal structure of HpFabZ-Emodin complex was also examined. The results showed that Emodin inhibition against HpFabZ could be implemented either through its occupying the entrance of the tunnel or embedding into the tunnel to prevent the substrate from accessing the active site.ConclusionOur work is expected to provide useful information for illumination of Emodin inhibition mechanism against HpFabZ, while Emodin itself could be used as a potential lead compound for further anti-bacterial drug discovery. |
| 语种 | 英语 |
| WOS记录号 | BMC:10.1186/1471-2180-9-91 |
| 出版者 | BioMed Central |
| 源URL | [http://119.78.100.183/handle/2S10ELR8/307073]  |
| 专题 | 新药研究国家重点实验室 |
| 通讯作者 | Guo,Yuewei; Shen,Xu |
| 作者单位 | 1.Chinese Academy of Sciences; Institute of Biochemistry and Cell Biology 2.Chinese Academy of Sciences; Drug Discovery and Design Center, State Key Laboratory of Drug Research, Shanghai Institute of Materia Medica |
| 推荐引用方式 GB/T 7714 | Chen,Jing,Zhang,Liang,Zhang,Yu,et al. Emodin targets the β-hydroxyacyl-acyl carrier protein dehydratase from Helicobacter pylori: enzymatic inhibition assay with crystal structural and thermodynamic characterization[J]. BMC Microbiology,2009,9(1). |
| APA | Chen,Jing.,Zhang,Liang.,Zhang,Yu.,Zhang,Haitao.,Du,Jiamu.,...&Shen,Xu.(2009).Emodin targets the β-hydroxyacyl-acyl carrier protein dehydratase from Helicobacter pylori: enzymatic inhibition assay with crystal structural and thermodynamic characterization.BMC Microbiology,9(1). |
| MLA | Chen,Jing,et al."Emodin targets the β-hydroxyacyl-acyl carrier protein dehydratase from Helicobacter pylori: enzymatic inhibition assay with crystal structural and thermodynamic characterization".BMC Microbiology 9.1(2009). |
入库方式： OAI收割
来源：上海药物研究所
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