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

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 dis...

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Autores principales: Goncalves, Victor, Brannigan, James A., Laporte, Alice, Bell, Andrew S., Roberts, Shirley M., Wilkinson, Anthony J., Leatherbarrow, Robin J., Tate, Edward W.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Royal Society of Chemistry 2016
Materias:
Chemistry
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5463734/
https://www.ncbi.nlm.nih.gov/pubmed/28626547
http://dx.doi.org/10.1039/c6md00531d
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author Goncalves, Victor
Brannigan, James A.
Laporte, Alice
Bell, Andrew S.
Roberts, Shirley M.
Wilkinson, Anthony J.
Leatherbarrow, Robin J.
Tate, Edward W.
author_facet Goncalves, Victor
Brannigan, James A.
Laporte, Alice
Bell, Andrew S.
Roberts, Shirley M.
Wilkinson, Anthony J.
Leatherbarrow, Robin J.
Tate, Edward W.
author_sort Goncalves, Victor
collection PubMed
description 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).
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spelling pubmed-54637342017-06-16 Structure-guided optimization of quinoline inhibitors of Plasmodium N-myristoyltransferase Goncalves, Victor Brannigan, James A. Laporte, Alice Bell, Andrew S. Roberts, Shirley M. Wilkinson, Anthony J. Leatherbarrow, Robin J. Tate, Edward W. Medchemcomm Chemistry 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). Royal Society of Chemistry 2016-11-11 /pmc/articles/PMC5463734/ /pubmed/28626547 http://dx.doi.org/10.1039/c6md00531d Text en This journal is © The Royal Society of Chemistry 2017 http://creativecommons.org/licenses/by/3.0/ This article is freely available. This article is licensed under a Creative Commons Attribution 3.0 Unported Licence (CC BY 3.0)
spellingShingle Chemistry
Goncalves, Victor
Brannigan, James A.
Laporte, Alice
Bell, Andrew S.
Roberts, Shirley M.
Wilkinson, Anthony J.
Leatherbarrow, Robin J.
Tate, Edward W.
Structure-guided optimization of quinoline inhibitors of Plasmodium N-myristoyltransferase
title Structure-guided optimization of quinoline inhibitors of Plasmodium N-myristoyltransferase
title_full Structure-guided optimization of quinoline inhibitors of Plasmodium N-myristoyltransferase
title_fullStr Structure-guided optimization of quinoline inhibitors of Plasmodium N-myristoyltransferase
title_full_unstemmed Structure-guided optimization of quinoline inhibitors of Plasmodium N-myristoyltransferase
title_short Structure-guided optimization of quinoline inhibitors of Plasmodium N-myristoyltransferase
title_sort structure-guided optimization of quinoline inhibitors of plasmodium n-myristoyltransferase
topic Chemistry
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5463734/
https://www.ncbi.nlm.nih.gov/pubmed/28626547
http://dx.doi.org/10.1039/c6md00531d
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