Identi�cation of an inhibitory pocket in falcilysin bound by chloroquine provides a new avenue for malaria drug development

HIGHLIGHTS

  • who: Posted Date February et al. from the Nanynag Technological University have published the article: Identi�cation of an inhibitory pocket in falcilysin bound by chloroquine provides a new avenue for malaria drug development, in the Journal: (JOURNAL)
  • what: The authors demonstrate that both drugs bind directly to a hydrophobic pocket and inhibit the function of a DV residing metalloprotease, falcilysin (FLN). While this approach has led to the discovery of the most important antimalarials in history such as the aminoquinolines (e_g, chloroquine, mefloquine, and piperaquine) and artemisinins (e_g, dihydroartesminin, artesunate, and artemether), it is . . .

     

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