Discovery of Novel and Ligand-Efficient Inhibitors of Plasmodium falciparum and Plasmodium vivaxN-Myristoyltransferase

[Image: see text] N-Myristoyltransferase (NMT) is an attractive antiprotozoan drug target. A lead-hopping approach was utilized in the design and synthesis of novel benzo[b]thiophene-containing inhibitors of Plasmodium falciparum (Pf) and Plasmodium vivax (Pv) NMT. These inhibitors are selective aga...

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Autores principales: Rackham, Mark D., Brannigan, James A., Moss, David K., Yu, Zhiyong, Wilkinson, Anthony J., Holder, Anthony A., Tate, Edward W., Leatherbarrow, Robin J.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Chemical Society 2012
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3601602/
https://www.ncbi.nlm.nih.gov/pubmed/23170970
http://dx.doi.org/10.1021/jm301474t
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author Rackham, Mark D.
Brannigan, James A.
Moss, David K.
Yu, Zhiyong
Wilkinson, Anthony J.
Holder, Anthony A.
Tate, Edward W.
Leatherbarrow, Robin J.
author_facet Rackham, Mark D.
Brannigan, James A.
Moss, David K.
Yu, Zhiyong
Wilkinson, Anthony J.
Holder, Anthony A.
Tate, Edward W.
Leatherbarrow, Robin J.
author_sort Rackham, Mark D.
collection PubMed
description [Image: see text] N-Myristoyltransferase (NMT) is an attractive antiprotozoan drug target. A lead-hopping approach was utilized in the design and synthesis of novel benzo[b]thiophene-containing inhibitors of Plasmodium falciparum (Pf) and Plasmodium vivax (Pv) NMT. These inhibitors are selective against Homo sapiens NMT1 (HsNMT), have excellent ligand efficiency (LE), and display antiparasitic activity in vitro. The binding mode of this series was determined by crystallography and shows a novel binding mode for the benzothiophene ring.
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spelling pubmed-36016022013-03-21 Discovery of Novel and Ligand-Efficient Inhibitors of Plasmodium falciparum and Plasmodium vivaxN-Myristoyltransferase Rackham, Mark D. Brannigan, James A. Moss, David K. Yu, Zhiyong Wilkinson, Anthony J. Holder, Anthony A. Tate, Edward W. Leatherbarrow, Robin J. J Med Chem [Image: see text] N-Myristoyltransferase (NMT) is an attractive antiprotozoan drug target. A lead-hopping approach was utilized in the design and synthesis of novel benzo[b]thiophene-containing inhibitors of Plasmodium falciparum (Pf) and Plasmodium vivax (Pv) NMT. These inhibitors are selective against Homo sapiens NMT1 (HsNMT), have excellent ligand efficiency (LE), and display antiparasitic activity in vitro. The binding mode of this series was determined by crystallography and shows a novel binding mode for the benzothiophene ring. American Chemical Society 2012-11-22 2013-01-10 /pmc/articles/PMC3601602/ /pubmed/23170970 http://dx.doi.org/10.1021/jm301474t Text en Copyright © 2012 American Chemical Society
spellingShingle Rackham, Mark D.
Brannigan, James A.
Moss, David K.
Yu, Zhiyong
Wilkinson, Anthony J.
Holder, Anthony A.
Tate, Edward W.
Leatherbarrow, Robin J.
Discovery of Novel and Ligand-Efficient Inhibitors of Plasmodium falciparum and Plasmodium vivaxN-Myristoyltransferase
title Discovery of Novel and Ligand-Efficient Inhibitors of Plasmodium falciparum and Plasmodium vivaxN-Myristoyltransferase
title_full Discovery of Novel and Ligand-Efficient Inhibitors of Plasmodium falciparum and Plasmodium vivaxN-Myristoyltransferase
title_fullStr Discovery of Novel and Ligand-Efficient Inhibitors of Plasmodium falciparum and Plasmodium vivaxN-Myristoyltransferase
title_full_unstemmed Discovery of Novel and Ligand-Efficient Inhibitors of Plasmodium falciparum and Plasmodium vivaxN-Myristoyltransferase
title_short Discovery of Novel and Ligand-Efficient Inhibitors of Plasmodium falciparum and Plasmodium vivaxN-Myristoyltransferase
title_sort discovery of novel and ligand-efficient inhibitors of plasmodium falciparum and plasmodium vivaxn-myristoyltransferase
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3601602/
https://www.ncbi.nlm.nih.gov/pubmed/23170970
http://dx.doi.org/10.1021/jm301474t
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