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Open AccessArticle

Anticancer Ruthenium Complexes with HDAC Isoform Selectivity

1
Department of Chemistry, Durham University, Lower Mountjoy, South Road, Durham DH1 3LE, UK
2
Department of Biosciences, Durham University, Stockton Road, Durham DH1 3LE, UK
*
Author to whom correspondence should be addressed.
Academic Editor: Kogularamanan Suntharalingam
Molecules 2020, 25(10), 2383; https://doi.org/10.3390/molecules25102383
Received: 20 April 2020 / Revised: 13 May 2020 / Accepted: 16 May 2020 / Published: 21 May 2020
(This article belongs to the Special Issue Metal Anticancer Complexes)
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. View Full-Text
Keywords: histone deacetylase inhibitors; ruthenium in medicine; selective enzyme inhibition histone deacetylase inhibitors; ruthenium in medicine; selective enzyme inhibition
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MDPI and ACS Style

Cross, J.M.; Blower, T.R.; Kingdon, A.D.H.; Pal, R.; Picton, D.M.; Walton, J.W. Anticancer Ruthenium Complexes with HDAC Isoform Selectivity. Molecules 2020, 25, 2383. https://doi.org/10.3390/molecules25102383

AMA Style

Cross JM, Blower TR, Kingdon ADH, Pal R, Picton DM, Walton JW. Anticancer Ruthenium Complexes with HDAC Isoform Selectivity. Molecules. 2020; 25(10):2383. https://doi.org/10.3390/molecules25102383

Chicago/Turabian Style

Cross, Jasmine M.; Blower, Tim R.; Kingdon, Alexander D.H.; Pal, Robert; Picton, David M.; Walton, James W. 2020. "Anticancer Ruthenium Complexes with HDAC Isoform Selectivity" Molecules 25, no. 10: 2383. https://doi.org/10.3390/molecules25102383

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