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

DOI: 10.1039/C6MD00531D DOI Help

Authors: Victor Goncalves (Imperial College London) , James A. Brannigan (University of York) , Alice Laporte (Imperial College London) , Andrew S. Bell (Imperial College London) , Shirley M. Roberts (University of York) , Anthony J. Wilkinson (University of York) , Robin J. Leatherbarrow (Imperial College London) , Edward W. Tate (Imperial College London)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Med. Chem. Commun.

State: Published (Approved)
Published: November 2016
Diamond Proposal Number(s): 1221 , 7864

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).

Subject Areas: Biology and Bio-materials, Chemistry, Medicine


Instruments: I02-Macromolecular Crystallography , I04-Macromolecular Crystallography