Potent inhibitors of the Plasmodium falciparum enzymes plasmepsin I and II devoid of cathepsin D inhibitory activity.

@article{Ersmark2004PotentIO,
  title={Potent inhibitors of the Plasmodium falciparum enzymes plasmepsin I and II devoid of cathepsin D inhibitory activity.},
  author={Karolina Ersmark and Isabella Feierberg and Sinisa Bjelic and Elizabeth Hamelink and Francine Hackett and Michael J. Blackman and Johan Hult{\'e}n and Bertil B. Samuelsson and Johan {\AA}qvist and Anders Hallberg},
  journal={Journal of medicinal chemistry},
  year={2004},
  volume={47 1},
  pages={
          110-22
        }
}
The hemoglobin-degrading aspartic proteases plasmepsin I (Plm I) and plasmepsin II (Plm II) of the malaria parasite Plasmodium falciparum have lately emerged as putative drug targets. A series of C(2)-symmetric compounds encompassing the 1,2-dihydroxyethylene scaffold and a variety of elongated P1/P1' side chains were synthesized via microwave-assisted palladium-catalyzed coupling reactions. Binding affinity calculations with the linear interaction energy method and molecular dynamics… CONTINUE READING
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