（SCI）Screening Peptide Inhibitors Using Phage Peptide Library with Isocitrate Lyase in Mycobacterium tuberculosis as Target
- 所属单位：化学与生命科学学院
- 教研室：化学与生命科学学院
- 发表刊物：CHEMICAL RESEARCH IN CHINESE UNIVERSITES
- 项目来源：自选课题
- 关键字：Mycobacterium tuberculosis Isocitrate lyase Gene expression Phage peptide library Peptide inhibitor
- 摘要：When devoured by macrophages, Mycobacterium tuberculosis remains persistent in macrophages and gains energy through the glyoxylate bypass to maintain its long-term existence in host cells. Therefore it is possible to stop persistent infections by interdicting the glyoxylate bypass in which the isocitrate lyase(ICL) is the key rate-limiting enzyme and a persistence factor. ICL is the target of anti-TB(TB: tubercular) drugs, which could screen ICL out and effectively inhibit the activity of ICL in Mycobacterium tuberculosis, and because of this, anti-TB drugs can be used to kill persistent Mycobacterium tuberculosis. In this study, the ICL gene of the Mycobacterium tuberculosis H37Rv was cloned successfully and recombinant protein with bioactivity was obtained through the enzyme characteristic appraisal. The specific activity of the recombined ICL is 24 μmol·mg–1 ·min–1. The recombined ICL protein was used as the target, and phages which can specifically combine to ICL were screened in the phage 7 peptide library. According to the results of the ELISA and DNA sequence detection, eventually three 7-peptide chains were synthesized. Then the peptide chains were reacted with ICL, respectively, to detect their inhibitory effects on ICL. The results show that all the three 7-peptide chains possessed varying inhibitory effects on the activity of ICL. This study provided lead compounds for the research and development of new peptide anti-TB drugs.
- 第一作者：殷玉和
- 论文类型：期刊论文
- 卷号：27
- 期号：4
- 页面范围：1
- 字数：1
- ISSN号：1005-9040
- 是否译文：否
- CN号：22-1183/O6
- 发表时间：2011-06-29
