Dimerization of a heat shock protein 90 inhibitor enhances inhibitory activity

被引：4

作者：

Wahyudi, Hendra ^{[1
]}

Wang, Yao ^{[1
]}

McAlpine, Shelli R. ^{[1
]}

机构：

[1] Univ New S Wales, Dept Chem, Sydney, NSW 2052, Australia

来源：

ORGANIC & BIOMOLECULAR CHEMISTRY | 2014年 / 12卷 / 05期

基金：

澳大利亚国家健康与医学研究理事会;

关键词：

SMALL-MOLECULE; SANSALVAMIDE; HSP90; CHAPERONE; DERIVATIVES; BINDING; HEAT-SHOCK-PROTEIN-90; CYTOTOXICITY; CONFORMATION; GELDANAMYCIN;

D O I：

10.1039/c3ob41722k

中图分类号：

O62 [有机化学];

学科分类号：

070303 ; 081704 ;

摘要：

Heat shock protein 90 (hsp90) accounts for 1-2% of the total proteins in normal cells and it functions as a dimer. Hsp90 behaves as a molecular chaperone that folds, assembles, and stabilizes client proteins. We have developed a novel hsp90 inhibitor, and herein we describe the synthesis and biological activity of the dimerized variant of this inhibitor. Tethering a monomer inhibitor together produced a dimerized compound that more effectively inhibits hsp90 over the monomer.

引用

页码：765 / 773

页数：9

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