A Review on Bacterial Cell division Protein and Recent Progress of FtsZ Inhibitors Development

被引:0
|
作者
Huang Xuan-He [1 ]
Sun Ning [2 ,3 ]
Zhong Dong-Xiao [1 ]
Chen Cui-Cui [1 ]
Li Ying [1 ]
Wong Wing-Leung [4 ]
Lu Yu-Jing [1 ]
机构
[1] Guangdong Univ Technol, Sch Biomed & Pharmaceut Sci, Guangzhou 510006, Peoples R China
[2] Hong Kong Polytech Univ, Dept Appl Biol Chem Technol, State Key Lab Chem Biol & Drug Discovery, Hong Kong, Peoples R China
[3] Guangzhou Med Univ, Affiliated Hosp 5, Guangzhou 510700, Peoples R China
[4] Wuyi Univ, Sch Biotechnol & Hlth Sci, Jiangmen 529020, Peoples R China
关键词
drug resistance bacteria; antibacterial agents; cell division protein FtsZ; FtsZ inhibitors; ESCHERICHIA-COLI; ANTIBACTERIAL ACTIVITY; STAPHYLOCOCCUS-AUREUS; ASSEMBLY DYNAMICS; THIAZOLE ORANGE; PEPTIDOGLYCAN SYNTHESIS; CRYSTAL-STRUCTURES; GTPASE ACTIVITY; TARGETING FTSZ; SMALL-MOLECULE;
D O I
10.16476/j.pibb.2020.0055
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
In recent years, the abuse of antibiotics has caused the emergence of drug-resistant bacteria, which is now widely spread around the world. It is currently a critical issue that seriously threats to human health due to the lack of effective clinical drugs to treat the multidrug-resistant bacterial infections. With such a serious shortage of drugs and means for clinical treatment against multidrug-resistant bacterial infections, it is urgently needed to develop new antibacterial drugs, especially those molecules possessing new mechanisms of action to combat the drug-resistant bacteria. Filamenting temperature-sensitive mutant Z (FtsZ) is an essential protein for bacterial division and has been one of the most popular targets for new drug discovery. FtsZ is a highly conserved protein and it plays a key role in cell division in most prokaryotic cells. In this article, we reviewed the structural characteristics and biological functions of bacterial cell division proteins and the recent research progress on antibacterial drugs development targeting FtsZ.
引用
收藏
页码:935 / 955
页数:21
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