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

Victor Goncalves*, James A. Brannigan, Alice Laporte, Andrew S. Bell, Shirley M. Roberts, Anthony J. Wilkinson, Robin J. Leatherbarrow, Edward W. Tate

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review


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).

Original languageEnglish
Pages (from-to)191-197
Number of pages7
Issue number1
Early online date11 Nov 2016
Publication statusPublished - 2017

Bibliographical note

© 2017, The Royal Society of Chemistry.

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