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Anticancer Ruthenium Complexes with HDAC Isoform Selectivity

The histone deacetylase (HDAC) enzymes have emerged as an important class of molecular targets in cancer therapy, with five inhibitors in clinical use. Recently, it has been shown that a lack of selectivity between the 11 Zn-dependent HDAC isoforms may lead to unwanted side-effects. In this paper, w...

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Autores principales: Cross, Jasmine M., Blower, Tim R., Kingdon, Alexander D. H., Pal, Robert, Picton, David M., Walton, James W.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7287671/
https://www.ncbi.nlm.nih.gov/pubmed/32455529
http://dx.doi.org/10.3390/molecules25102383
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author Cross, Jasmine M.
Blower, Tim R.
Kingdon, Alexander D. H.
Pal, Robert
Picton, David M.
Walton, James W.
author_facet Cross, Jasmine M.
Blower, Tim R.
Kingdon, Alexander D. H.
Pal, Robert
Picton, David M.
Walton, James W.
author_sort Cross, Jasmine M.
collection PubMed
description The histone deacetylase (HDAC) enzymes have emerged as an important class of molecular targets in cancer therapy, with five inhibitors in clinical use. Recently, it has been shown that a lack of selectivity between the 11 Zn-dependent HDAC isoforms may lead to unwanted side-effects. In this paper, we show that piano stool Ru complexes can act as HDAC inhibitors, and variation in the capping arene leads to differences in HDAC isoform selectivity.
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spelling pubmed-72876712020-06-15 Anticancer Ruthenium Complexes with HDAC Isoform Selectivity Cross, Jasmine M. Blower, Tim R. Kingdon, Alexander D. H. Pal, Robert Picton, David M. Walton, James W. Molecules Article The histone deacetylase (HDAC) enzymes have emerged as an important class of molecular targets in cancer therapy, with five inhibitors in clinical use. Recently, it has been shown that a lack of selectivity between the 11 Zn-dependent HDAC isoforms may lead to unwanted side-effects. In this paper, we show that piano stool Ru complexes can act as HDAC inhibitors, and variation in the capping arene leads to differences in HDAC isoform selectivity. MDPI 2020-05-21 /pmc/articles/PMC7287671/ /pubmed/32455529 http://dx.doi.org/10.3390/molecules25102383 Text en © 2020 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Cross, Jasmine M.
Blower, Tim R.
Kingdon, Alexander D. H.
Pal, Robert
Picton, David M.
Walton, James W.
Anticancer Ruthenium Complexes with HDAC Isoform Selectivity
title Anticancer Ruthenium Complexes with HDAC Isoform Selectivity
title_full Anticancer Ruthenium Complexes with HDAC Isoform Selectivity
title_fullStr Anticancer Ruthenium Complexes with HDAC Isoform Selectivity
title_full_unstemmed Anticancer Ruthenium Complexes with HDAC Isoform Selectivity
title_short Anticancer Ruthenium Complexes with HDAC Isoform Selectivity
title_sort anticancer ruthenium complexes with hdac isoform selectivity
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7287671/
https://www.ncbi.nlm.nih.gov/pubmed/32455529
http://dx.doi.org/10.3390/molecules25102383
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