Histone deacetylases (HDACs) are enzymes that mediate the removal of acetyl groups from numerous acetylated proteins (including histones) and some are associated with the cell cycle, inflammation, apoptosis and cancer. HDACs have been found to be involved in a wide range of diseases and conditions and represent promising drug targets.  There are eleven zinc-binding mammalian HDACs including 4 class I, 4 class IIa and 2 class IIb proteins.

The Fairlie Research Group at The University of Queensland (UQ) has exploited structural differences between Class I and IIa HDACs to develop two generations of new compounds that are potent and selective inhibitors of class IIa HDACs.

Inhibitors of Class IIa HDACs have the potential to treat many inflammation-related pathologies.

Key features

  • New potent and selective inhibitors of class IIa HDAC enzymes
  • No induction of cellular histone H4 acetylation, unlike most inhibitors of HDACs
  • Potential for modulating class IIa HDAC functions in vivo with fewer cytotoxic side effects than other HDAC inhibitors.

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