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Issue 12, 2014
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An azumamide C analogue without the zinc-binding functionality

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Abstract

Histone deacetylase (HDAC) inhibitors have attracted considerable attention due to their promise as therapeutic agents. Most HDAC inhibitors adhere to a general “cap-linker-Zn2+-binding group” architecture but recent studies have indicated that potent inhibition may be achieved without a Zn2+-coordinating moiety. Herein, we describe the synthesis of an azumamide analogue lacking its native Zn2+-binding group and evaluation of its inhibitory activity against recombinant human HDAC1–11. Furthermore, kinetic investigation of the inhibitory mechanism of both parent natural product and synthetic analogue against HDAC3-NCoR2 is reported as well as their activity against Burkitt's lymphoma cell proliferation.

Graphical abstract: An azumamide C analogue without the zinc-binding functionality

  • This article is part of the themed collection: Epigenetics
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Publication details

The article was received on 13 Jun 2014, accepted on 11 Aug 2014 and first published on 12 Aug 2014


Article type: Concise Article
DOI: 10.1039/C4MD00252K
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Med. Chem. Commun., 2014,5, 1849-1855

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    An azumamide C analogue without the zinc-binding functionality

    J. S. Villadsen, B. Kitir, K. Wich, T. Friis, A. S. Madsen and C. A. Olsen, Med. Chem. Commun., 2014, 5, 1849
    DOI: 10.1039/C4MD00252K

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