Lead discovery of inhibitors of the dihydrofolate reductase domain of Plasmodium falciparum dihydrofolate reductase-thymidylate synthase.

@article{Toyoda1997LeadDO,
  title={Lead discovery of inhibitors of the dihydrofolate reductase domain of Plasmodium falciparum dihydrofolate reductase-thymidylate synthase.},
  author={Takuya Toyoda and R K Brobey and Go Sano and Toshihiro Horii and Nobuo Tomioka and Akiko Itai},
  journal={Biochemical and biophysical research communications},
  year={1997},
  volume={235 3},
  pages={515-9}
}
A three-dimensional structure model of the dihydrofolate reductase (DHFR) domain of the bifunctional DHFR-thymidylate synthase of Plasmodium falciparum was used as a basis for computational screening of commercially available compounds for candidate inhibitors. Compounds which can stably dock to the model with strong ionic hydrogen bonds via protonation by an aspartic acid residue at the bottom of the active site were identified through docking simulation. Among compounds thus identified, 21… CONTINUE READING