Anticancer Ruthenium Complexes with HDAC Isoform Selectivity
by
Jasmine M. Cross 1, Tim R. Blower 2
, Alexander D. H. Kingdon 1, Robert Pal 1, David M. Picton 2 and James W. Walton 1,*
Jasmine M. Cross 1, Tim R. Blower 2, Alexander D. H. Kingdon 1, Robert Pal 1, David M. Picton 2 and James W. Walton 1,*
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.
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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.
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