Structure-guided optimization of quinoline inhibitors of Plasmodium N-myristoyltransferaseThe authors declare no competing interests.Electronic supplementary information (ESI) available: Synthesis details and structural characterization of compounds, X-ray data collection and statistics, supplementary Fig. S1-S6. See DOI: 10.1039/c6md00531d

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). Quinolines with balanced activities against both Plasmodium vivax and Plasmodium falciparum N -myristoyltransferase were identified.