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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...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2020
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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. |
format | Online Article Text |
id | pubmed-7287671 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
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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