Design, synthesis and biological assay of novel tripeptidic tetrazoles as inhibitors of 20S proteasome.
- Author:
Yu-Heng MA
1
;
Bo XU
;
Jing-Rong CUI
;
Zhen-Jun YANG
;
Liang-Ren ZHANG
;
Li-He ZHANG
Author Information
1. State Key Laboratory of Natural and Biomimetic Drugs, School of Pharmaceutical Sciences, Peking University, Beijing 100091, China.
- Publication Type:Journal Article
- MeSH:
Biological Assay;
Drug Design;
Molecular Structure;
Oligopeptides;
chemical synthesis;
chemistry;
pharmacology;
Proteasome Endopeptidase Complex;
chemistry;
Proteasome Inhibitors;
chemical synthesis;
chemistry;
pharmacology;
Tetrazoles;
chemical synthesis;
chemistry;
pharmacology
- From:
Acta Pharmaceutica Sinica
2012;47(4):472-478
- CountryChina
- Language:Chinese
-
Abstract:
Ubiquitin-proteasome pathway (UPP) is one of the ways utilized for selective degradation of many proteins in cells, and the 20S proteasome takes the functional machinery where hydrolysis of targeted proteins takes place. Based on existing peptide inhibitors, a series of novel tripeptidic tetrazoles have been designed, synthesized, and the structures have been confirmed with 1H NMR, MS and elemental analysis. Among them, three compounds (6b, 6d and 6h) showed inhibitory activities of ChT-L of 20S proteasome.
