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Issue 12, 2014
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Evaluation of functional groups as acetyl-lysine mimetics for BET bromodomain inhibition

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Abstract

The ability of various functional groups to engage the acetyl-lysine (KAc) binding site within bromo- and extra-terminal domain (BET) protein family members BRD2, BRD3 and BRD4 was evaluated by screening small molecular fragments – coupled to a known arylsulfonamide scaffold – in biochemical inhibition assays. Useful structure activity relationships have been established and novel functional groups that bind to the KAc binding pocket identified. Additional microsomal degradation studies were also undertaken revealing significant differences in metabolic stability between two commonly employed BET inhibitor fragments.

Graphical abstract: Evaluation of functional groups as acetyl-lysine mimetics for BET bromodomain inhibition

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

The article was received on 23 Apr 2014, accepted on 20 Jun 2014 and first published on 23 Jun 2014


Article type: Concise Article
DOI: 10.1039/C4MD00182F
Citation: Med. Chem. Commun., 2014,5, 1834-1842
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    Evaluation of functional groups as acetyl-lysine mimetics for BET bromodomain inhibition

    P. P. Sharp, J. Garnier, D. C. S. Huang and C. J. Burns, Med. Chem. Commun., 2014, 5, 1834
    DOI: 10.1039/C4MD00182F

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