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

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Title: Structure-guided optimization of quinoline inhibitors of Plasmodium N-myristoyltransferase
Authors: Goncalves, V
Brannigan, JA
Laporte, A
Bell, AS
Roberts, SM
Wilkinson, AJ
Leatherbarrow, RJ
Tate, EW
Item Type: Journal Article
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).
Issue Date: 11-Nov-2016
Date of Acceptance: 9-Nov-2016
URI: http://hdl.handle.net/10044/1/43036
DOI: https://dx.doi.org/10.1039/C6MD00531D
ISSN: 2040-2511
Publisher: Royal Society of Chemistry
Start Page: 191
End Page: 197
Journal / Book Title: MedChemComm
Volume: 8
Copyright Statement: This article is licensed under a Creative Commons Attribution 3.0 Unported Licence.
Sponsor/Funder: Wellcome Trust
Medical Research Council (MRC)
Funder's Grant Number: 087792/B/08/Z
G0900278
Keywords: Science & Technology
Life Sciences & Biomedicine
Biochemistry & Molecular Biology
Chemistry, Medicinal
Pharmacology & Pharmacy
POTENTIAL-DRUG TARGET
MYRISTOYL-COA
SELECTIVE INHIBITORS
VIVAX MALARIA
DISCOVERY
DESIGN
LIGAND
LEISHMANIASIS
FALCIPARUM
PARASITES
0304 Medicinal And Biomolecular Chemistry
0305 Organic Chemistry
1115 Pharmacology And Pharmaceutical Sciences
Notes: crosscheck: This document is CrossCheck deposited related_data: Supplementary Information identifier: Victor Goncalves (ResearcherID) copyright_licence: The Royal Society of Chemistry has an exclusive publication licence for this journal history: Received 20 September 2016; Accepted 9 November 2016; Accepted Manuscript published 11 November 2016; Advance Article published 18 November 2016
Publication Status: Published
Appears in Collections:Chemistry
Biological and Biophysical Chemistry
Faculty of Natural Sciences