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

Victor Goncalves 1, * James A. Brannigan 2 Alice Laporte 1 Andrew S. Bell 1 Shirley M. Roberts 2 Anthony J. Wilkinson 2 Robin J. Leatherbarrow 1 Edward W. Tate 1, *
* Auteur correspondant
1 Department of Chemistry [Imperial College London]
2 Structural Biology Laboratory, Department of Chemistry, University of York
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).
Keywords : potential-drug target myristoyl-coa selective inhibitors vivax malaria discovery design ligand leishmaniasis falciparum parasites
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https://hal-univ-bourgogne.archives-ouvertes.fr/hal-01496799
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Soumis le : lundi 27 mars 2017 - 19:09:17
Dernière modification le : lundi 27 mars 2017 - 19:11:34

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Victor Goncalves, James A. Brannigan, Alice Laporte, Andrew S. Bell, Shirley M. Roberts, et al.. Structure-guided optimization of quinoline inhibitors of Plasmodium N-myristoyltransferase. MedChemComm, Royal Society of Chemistry, 2017, 8 (1), pp.191 - 197. ⟨10.1039/C6MD00531D⟩. ⟨hal-01496799⟩

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