Emodin targets the beta-hydroxyacyl-acyl carrier protein dehydratase from Helicobacter pylori: enzymatic inhibition assay with crystal structural and thermodynamic characterization

	Emodin targets the beta-hydroxyacyl-acyl carrier protein dehydratase from Helicobacter pylori: enzymatic inhibition assay with crystal structural and thermodynamic characterization
	Chen, J; Zhang, L; Zhang, Y; Zhang, HT; Du, JM; Ding, JP; Guo, YW; Jiang, HL; Shen, X
刊名	BMC MICROBIOLOGY
	2009
卷号	9 期号:1 页码:91-91
通讯作者	Guo, YW (reprint author), Chinese Acad Sci, Drug Discovery & Design Ctr, State Key Lab Drug Res, Shanghai Inst Mat Med, Shanghai 201203, Peoples R China.,jingchen@mail.shcnc.ac.cn ; zhangliang1980@gmail.com ; octopus_xzy@hotmail.com ; kevin.htzhang@gmail.com ; jmdu@sibs.ac.cn ; jpding@sibs.ac.cn ; ywguo@mail.shcnc.ac.cn ; hljiang@mail.shcnc.ac.cn ; xshen@mail.shcnc.ac.cn
英文摘要	Background: The 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. Results: Here we reported that Emodin functioned as a competitive inhibitor against the recombinant beta-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. Conclusion: Our 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.
学科主题	Microbiology
类目[WOS]	Microbiology
关键词[WOS]	TYROSINE KINASE INHIBITOR ; POLYGONUM-HYPOLEUCUM OHWI ; FATTY-ACID BIOSYNTHESIS ; CANCER CELLS ; BREAST-CANCER ; DNA-DAMAGE ; FABZ ; PROLIFERATION ; ERADICATION ; FLAVONOIDS
收录类别	SCI
语种	英语
WOS记录号	WOS:000266803000001
内容类型	期刊论文
版本	出版稿
源URL	[http://202.127.25.143/handle/331003/1310]
专题	上海生化细胞研究所_上海生科院生化细胞研究所
推荐引用方式 GB/T 7714	Chen, J,Zhang, L,Zhang, Y,et al. Emodin targets the beta-hydroxyacyl-acyl carrier protein dehydratase from Helicobacter pylori: enzymatic inhibition assay with crystal structural and thermodynamic characterization[J]. BMC MICROBIOLOGY,2009,9(1):91-91.
APA	Chen, J.,Zhang, L.,Zhang, Y.,Zhang, HT.,Du, JM.,...&Shen, X.(2009).Emodin targets the beta-hydroxyacyl-acyl carrier protein dehydratase from Helicobacter pylori: enzymatic inhibition assay with crystal structural and thermodynamic characterization.BMC MICROBIOLOGY,9(1),91-91.
MLA	Chen, J,et al."Emodin targets the beta-hydroxyacyl-acyl carrier protein dehydratase from Helicobacter pylori: enzymatic inhibition assay with crystal structural and thermodynamic characterization".BMC MICROBIOLOGY 9.1(2009):91-91.