Anticancer ruthenium complexes with HDAC isoform selectivity

Jasmine M. Cross; Tim R. Blower; Alex Kingdon; Robert Pal; David M. Picton; James W. Walton

doi:10.3390/molecules25102383

Anticancer ruthenium complexes with HDAC isoform selectivity

Jasmine M. Cross
, Tim R. Blower
, Alex Kingdon
, Robert Pal
, David M. Picton
, James W. Walton

Durham University

Research output: Contribution to journal › Article › peer-review

10 Citations (Scopus)

Abstract

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.

Original language	English
Article number	2383
Journal	Molecules
Volume	25
Issue number	10
DOIs	https://doi.org/10.3390/molecules25102383
Publication status	Published - 1 May 2020
Externally published	Yes

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

SDG 3 Good Health and Well-being

Keywords

Histone deacetylase inhibitors
Ruthenium in medicine
Selective enzyme inhibition

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10.3390/molecules25102383Licence: CC BY

Cite this

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title = "Anticancer ruthenium complexes with HDAC isoform selectivity",

abstract = "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.",

keywords = "Histone deacetylase inhibitors, Ruthenium in medicine, Selective enzyme inhibition",

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AU - Cross, Jasmine M.

AU - Blower, Tim R.

AU - Kingdon, Alex

AU - Pal, Robert

AU - Picton, David M.

AU - Walton, James W.

PY - 2020/5/1

Y1 - 2020/5/1

N2 - 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.

AB - 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.

KW - Histone deacetylase inhibitors

KW - Ruthenium in medicine

KW - Selective enzyme inhibition

U2 - 10.3390/molecules25102383

DO - 10.3390/molecules25102383

M3 - Article

SN - 1420-3049

VL - 25

JO - Molecules

JF - Molecules

IS - 10

M1 - 2383

ER -

Anticancer ruthenium complexes with HDAC isoform selectivity

Abstract

UN SDGs

Keywords

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