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

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JournalMedChemComm
DateAccepted/In press - 9 Nov 2016
DateE-pub ahead of print - 11 Nov 2016
DatePublished (current) - 2017
Issue number1
Volume8
Number of pages7
Pages (from-to)191-197
Early online date11/11/16
Original languageEnglish

Abstract

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).

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© 2017, The Royal Society of Chemistry.

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