Structure-guided optimization of quinoline inhibitors of Plasmodium N-myristoyltransferase.
Fiche publication
Date publication
janvier 2017
Journal
MedChemComm
Auteurs
Membres identifiés du Cancéropôle Est :
Dr GONCALVES Victor
Tous les auteurs :
Goncalves V, Brannigan JA, Laporte A, Bell AS, Roberts SM, Wilkinson AJ, Leatherbarrow RJ, Tate EW
Lien Pubmed
Résumé
The parasite Plasmodium vivax is the most widely distributed cause of recurring malaria. N-Myristoyltransferase (NMT), an enzyme that catalyses the covalent attachment of myristate to the N-terminal glycine of substrate proteins, has been described as a potential target for the treatment of this disease. Herein, we report the synthesis and the structure-guided optimization of a series of quinolines with balanced activity against both Plasmodium vivax and Plasmodium falciparum N-myristoyltransferase (NMT).
Référence
Medchemcomm. 2017 Jan;8(1):191-197