Structure-guided optimization of quinoline inhibitors of Plasmodium N-myristoyltransferase.

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

https://www.ncbi.nlm.nih.gov/pubmed/28626547

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