Structure-guided optimization of quinoline inhibitors of Plasmodium N-myristoyltransferase
File(s)c6md00531d.pdf (1.2 MB) Manuscript MD-RES-09-2016-000531 Revised.docx (5.95 MB)
Published version
Accepted version
Author(s)
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).
Date Issued
2016-11-11
Date Acceptance
2016-11-09
Citation
MedChemComm, 2016, 8, pp.191-197
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.
License URL
Sponsor
Wellcome Trust
Medical Research Council (MRC)
Grant Number
087792/B/08/Z
G0900278
Subjects
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