Discovery of high affinity inhibitors of Leishmania donovani N-myristoyltransferase

N-Myristoyltransferase (NMT) is a potential drug target in Leishmania parasites. Scaffold-hopping from published inhibitors yielded the serendipitous discovery of a chemotype selective for Leishmania donovani NMT; development led to high affinity inhibitors with excellent ligand efficiency. The bind...

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Autores principales: Rackham, Mark D., Yu, Zhiyong, Brannigan, James A., Heal, William P., Paape, Daniel, Barker, K. Victoria, Wilkinson, Anthony J., Smith, Deborah F., Leatherbarrow, Robin J., Tate, Edward W.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Royal Society of Chemistry 2015
Materias:
Chemistry
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4757855/
https://www.ncbi.nlm.nih.gov/pubmed/26962429
http://dx.doi.org/10.1039/c5md00241a
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author Rackham, Mark D.
Yu, Zhiyong
Brannigan, James A.
Heal, William P.
Paape, Daniel
Barker, K. Victoria
Wilkinson, Anthony J.
Smith, Deborah F.
Leatherbarrow, Robin J.
Tate, Edward W.
author_facet Rackham, Mark D.
Yu, Zhiyong
Brannigan, James A.
Heal, William P.
Paape, Daniel
Barker, K. Victoria
Wilkinson, Anthony J.
Smith, Deborah F.
Leatherbarrow, Robin J.
Tate, Edward W.
author_sort Rackham, Mark D.
collection PubMed
description N-Myristoyltransferase (NMT) is a potential drug target in Leishmania parasites. Scaffold-hopping from published inhibitors yielded the serendipitous discovery of a chemotype selective for Leishmania donovani NMT; development led to high affinity inhibitors with excellent ligand efficiency. The binding mode was characterised by crystallography and provides a structural rationale for selectivity.
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spelling pubmed-47578552016-03-07 Discovery of high affinity inhibitors of Leishmania donovani N-myristoyltransferase Rackham, Mark D. Yu, Zhiyong Brannigan, James A. Heal, William P. Paape, Daniel Barker, K. Victoria Wilkinson, Anthony J. Smith, Deborah F. Leatherbarrow, Robin J. Tate, Edward W. Medchemcomm Chemistry N-Myristoyltransferase (NMT) is a potential drug target in Leishmania parasites. Scaffold-hopping from published inhibitors yielded the serendipitous discovery of a chemotype selective for Leishmania donovani NMT; development led to high affinity inhibitors with excellent ligand efficiency. The binding mode was characterised by crystallography and provides a structural rationale for selectivity. Royal Society of Chemistry 2015-10-08 2015-08-19 /pmc/articles/PMC4757855/ /pubmed/26962429 http://dx.doi.org/10.1039/c5md00241a Text en This journal is © The Royal Society of Chemistry 2015 http://creativecommons.org/licenses/by/3.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution 3.0 Unported License (http://creativecommons.org/licenses/by/3.0/) which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Chemistry
Rackham, Mark D.
Yu, Zhiyong
Brannigan, James A.
Heal, William P.
Paape, Daniel
Barker, K. Victoria
Wilkinson, Anthony J.
Smith, Deborah F.
Leatherbarrow, Robin J.
Tate, Edward W.
Discovery of high affinity inhibitors of Leishmania donovani N-myristoyltransferase
title Discovery of high affinity inhibitors of Leishmania donovani N-myristoyltransferase
title_full Discovery of high affinity inhibitors of Leishmania donovani N-myristoyltransferase
title_fullStr Discovery of high affinity inhibitors of Leishmania donovani N-myristoyltransferase
title_full_unstemmed Discovery of high affinity inhibitors of Leishmania donovani N-myristoyltransferase
title_short Discovery of high affinity inhibitors of Leishmania donovani N-myristoyltransferase
title_sort discovery of high affinity inhibitors of leishmania donovani n-myristoyltransferase
topic Chemistry
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4757855/
https://www.ncbi.nlm.nih.gov/pubmed/26962429
http://dx.doi.org/10.1039/c5md00241a
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