Identification of phosphinate dipeptide analog inhibitors directed against the Plasmodium falciparum M17 leucine aminopeptidase as lead antimalarial compounds.

@article{SkinnerAdams2007IdentificationOP,
  title={Identification of phosphinate dipeptide analog inhibitors directed against the Plasmodium falciparum M17 leucine aminopeptidase as lead antimalarial compounds.},
  author={Tina S. Skinner-Adams and Jonathan P Lowther and F. Teuscher and Colin M. Stack and J. Grembecka and Artur Mucha and Pawel Kafarski and Katharine Trenholme and John Pius Dalton and Donald L. Gardiner},
  journal={Journal of medicinal chemistry},
  year={2007},
  volume={50 24},
  pages={6024-31}
}
Previous studies have pinpointed the M17 leucyl aminopeptidase of Plasmodium falciparum (PfLAP) as a target for the development of new antimalarials. This metallo-exopeptidase functions in the terminal stages of hemoglobin digestion and is inhibited by bestatin, a natural analog of Phe-Leu. By screening novel phosphinate dipeptide analogues for inhibitory activity against recombinant PfLAP, we have discovered two compounds, 4 (hPheP[CH2]Phe) and 5 (hPheP[CH2]Tyr), with inhibitory constants… CONTINUE READING

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