[Design, synthesis and biological assay of novel tripeptidic tetrazoles as inhibitors of 20S proteasome].
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.
State Key Laboratory of Natural and Biomimetic Drugs, School of Pharmaceutical Sciences, Peking University, Beijing 100091, China.
Yu-Heng
YH
Ma
Bo
B
Xu
Jing-Rong
JR
Cui
Zhen-Jun
ZJ
Yang
Liang-Ren
LR
Zhang
Li-He
LH
Zhang
D001681:Biological Assay; D015195:Drug Design; D015394:Molecular Structure; D009842:Oligopeptides / Q000138:chemical synthesis* / Q000737:chemistry / Q000494:pharmacology; D046988:Proteasome Endopeptidase Complex / Q000737:chemistry*; D061988:Proteasome Inhibitors / Q000138:chemical synthesis* / Q000737:chemistry / Q000494:pharmacology; D013777:Tetrazoles / Q000138:chemical synthesis* / Q000737:chemistry / Q000494:pharmacology
D009842:Oligopeptides; D061988:Proteasome Inhibitors; D013777:Tetrazoles; D046988:Proteasome Endopeptidase Complex