文献类型：期刊文献

英文题名：Caffeic acid phenethyl ester (CAPE), an active component of propolis, inhibits Helicobacter pylori peptide deformylase activity

作者：Cui, Kunqiang[1];Lu, Weiqiang[1];Zhu, Lili[1];Shen, Xu[1,2];Huang, Jin[1]

机构：[1]E China Univ Sci & Technol, Sch Pharm, Shanghai Key Lab Chem Biol, Shanghai Key Lab New Drug Design, Shanghai 200237, Peoples R China;[2]Chinese Acad Sci, Shanghai Inst Mat Med, Shanghai 201203, Peoples R China

年份：2013

卷号：435

期号：2

起止页码：289

外文期刊名：BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS

收录：;WOS:【SCI-EXPANDED(收录号:WOS:000320828300021)】；

基金：This work was supported by the National Natural Science Foundation of China (Grant 81102420), the Innovation Program of Shanghai Municipal Education Commission (Grant 10ZZ41), the Specialized Research Fund for the Doctoral Program of Higher Education of China (Grant 20090074120012), the Shanghai Committee of Science and Technology (Grant 11DZ2260600), and the Fundamental Research Funds for the Central Universities.

语种：英文

外文关键词：Helicobacter pylori; Peptide deformylase; Propolis; Phenolic compounds; Caffeic acid phenethyl ester

摘要：Helicobacter pylori (H. pylori) is a major causative factor for gastrointestinal illnesses, H. pylori peptide deformylase (HpPDF) catalyzes the removal of formyl group from the N-terminus of nascent polypeptide chains, which is essential for H. pylori survival and is considered as a promising drug target for anti-H. pylori therapy. Propolis, a natural antibiotic from honeybees, is reported to have an inhibitory effect on the growth of H. pylori in vitro. In addition, previous studies suggest that the main active constituents in the propolis are phenolic compounds. Therefore, we evaluated a collection of phenolic compounds derived from propolis for enzyme inhibition against HpPDF. Our study results show that Caffeic acid phenethyl ester (CAPE), one of the main medicinal components of propolis, is a competitive inhibitor against HpPDF, with an IC50 value of 4.02 mu M. Furthermore, absorption spectra and crystal structural characterization revealed that different from most well known PDF inhibitors, CAPE block the substrate entrance, preventing substrate from approaching the active site, but CAPE does not have chelate interaction with HpPDF and does not disrupt the metal-dependent catalysis. Our study provides valuable information for understanding the potential anti-H. pylori mechanism of propolis, and CAPE could be served as a lead compound for further anti-H. pylori drug discovery. Crown Copyright (C) 2013 Published by Elsevier Inc. All rights reserved.