Select pyrimidinones inhibit the propagation of the malarial parasite, Plasmodium falciparum

Bioorg Med Chem. 2009 Feb 15;17(4):1527-33. doi: 10.1016/j.bmc.2009.01.024. Epub 2009 Jan 20.

Abstract

Plasmodium falciparum, the Apicomplexan parasite that is responsible for the most lethal forms of human malaria, is exposed to radically different environments and stress factors during its complex lifecycle. In any organism, Hsp70 chaperones are typically associated with tolerance to stress. We therefore reasoned that inhibition of P. falciparum Hsp70 chaperones would adversely affect parasite homeostasis. To test this hypothesis, we measured whether pyrimidinone-amides, a new class of Hsp70 modulators, could inhibit the replication of the pathogenic P. falciparum stages in human red blood cells. Nine compounds with IC(50) values from 30 nM to 1.6 micrOM were identified. Each compound also altered the ATPase activity of purified P. falciparum Hsp70 in single-turnover assays, although higher concentrations of agents were required than was necessary to inhibit P. falciparum replication. Varying effects of these compounds on Hsp70s from other organisms were also observed. Together, our data indicate that pyrimidinone-amides constitute a novel class of anti-malarial agents.

Publication types

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

MeSH terms

  • Adenosine Triphosphatases / antagonists & inhibitors
  • Adenosine Triphosphatases / metabolism
  • Amides / pharmacology
  • Animals
  • Antimalarials / pharmacology*
  • Erythrocytes / parasitology
  • HSP70 Heat-Shock Proteins / antagonists & inhibitors*
  • HSP70 Heat-Shock Proteins / metabolism
  • Humans
  • Malaria, Falciparum / drug therapy
  • Malaria, Falciparum / parasitology
  • Models, Molecular
  • Parasitic Sensitivity Tests
  • Plasmodium falciparum / drug effects*
  • Plasmodium falciparum / metabolism
  • Pyrimidinones / pharmacology*

Substances

  • Amides
  • Antimalarials
  • HSP70 Heat-Shock Proteins
  • Pyrimidinones
  • Adenosine Triphosphatases