Identification and characterization of small molecule inhibitors of a class I histone deacetylase from Plasmodium falciparum

J Med Chem. 2009 Apr 23;52(8):2185-7. doi: 10.1021/jm801654y.

Abstract

A library of approximately 2000 small molecules biased toward inhibition of histone deacetylases was assayed for antimalarial activity in a high-throughput P. falciparum viability assay. Active compounds were cross-analyzed for induction of histone hyperacetylation in a human myeloma cell line to identify HDAC inhibitors with selectivity for P. falciparum over the human host. To verify on-target selectivity, pfHDAC-1 was expressed and purified and a biochemical assay for pfHDAC-1 activity was established.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Acetylation
  • Animals
  • Antimalarials / chemistry*
  • Antimalarials / pharmacology
  • Cell Line, Tumor
  • Histone Deacetylase Inhibitors*
  • Histone Deacetylases / chemistry
  • Humans
  • Kinetics
  • Parasitic Sensitivity Tests
  • Plasmodium falciparum / drug effects
  • Plasmodium falciparum / enzymology*
  • Recombinant Proteins / antagonists & inhibitors
  • Recombinant Proteins / chemistry
  • Small Molecule Libraries*
  • Structure-Activity Relationship

Substances

  • Antimalarials
  • Histone Deacetylase Inhibitors
  • Recombinant Proteins
  • Small Molecule Libraries
  • Histone Deacetylases