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Issue 5, 2014
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Dimerization of a heat shock protein 90 inhibitor enhances inhibitory activity

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Abstract

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.

Graphical abstract: Dimerization of a heat shock protein 90 inhibitor enhances inhibitory activity

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Publication details

The article was received on 22 Aug 2013, accepted on 05 Nov 2013 and first published on 06 Nov 2013


Article type: Paper
DOI: 10.1039/C3OB41722K
Org. Biomol. Chem., 2014,12, 765-773

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    Dimerization of a heat shock protein 90 inhibitor enhances inhibitory activity

    H. Wahyudi, Y. Wang and S. R. McAlpine, Org. Biomol. Chem., 2014, 12, 765
    DOI: 10.1039/C3OB41722K

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