Inside HDAC with HDAC inhibitors
Abstract
Histone deacetylase inhibitors are a large group of diverse molecules intrinsically able to inhibit cell proliferation in various cancer cell lines. Their apoptotic effects have been linked to the modulation in the expression of several regulatory tumor suppressor genes caused by the modified status of histone acetylation, a key event in chromatin remodelling. As the initial histone deacetylase activity of HDAC has been extended to other proteins, the possible other biological mechanisms modified by HDAC inhibitor treatments are still to be clarified. The need for HDAC isoform selective inhibitors is an important issue to serve this goal. This review discusses the approaches proposed by several research groups working on the synthesis of HDAC inhibitors, based on modelling studies and the way these findings were used to obtain new HDAC inhibitors with possible isoform selectivity.
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Previous reports postulate that an intramolecular hydrogen bond between the amine and carbonyl must be broken to permit successful zinc chelation, and a desolvation penalty is paid for this rearrangement.
“This is consistent with previous reports postulating that an intramolecular hydrogen bond between the amine and carbonyl must be broken to permit successful zinc chelation, and a desolvation penalty is paid for this rearrangement to occur (1, 25-28, 34).”
From Histone Deacetylase (HDAC) Inhibitor Kinetic Rate Constants Correlate with Cellular Histone Acetylation but Not Transcription and Cell Viability (2013) · cites this paper as [25]
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References 103 · Cited by 363
- Authors
- Bertrand, P.
- Affiliations
- Centre National de la Recherche Scientifique (FR)
- Corresponding author
- Bertrand, Philippe
- Venue
- European Journal of Medicinal Chemistry
- Publisher
- Elsevier BV
- Published
- 2010-06
- Volume
- 45
- Issue
- 6
- Pages
- 2095-2116
- ISSN
- 0223-5234 (ISSN-L)
- OpenAlex
- W2059914085
- Cited by
- 363
- References
- 103
- Citations by year
- 2026: 12 · 2025: 16 · 2024: 17 · 2023: 18 · 2022: 15 · 2021: 27 · 2020: 17 · 2019: 27 · 2018: 26 · 2017: 20 · 2016: 20 · 2015: 27 · 2014: 32 · 2013: 29 · 2012: 31
- FWCI
- 2.72
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- European Journal of Medicinal Chemistry (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Histone Deacetylase Inhibitors Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Enzyme function and inhibition
- Physical Sciences › Chemistry › Organic Chemistry › Synthesis and biological activity
- Keywords
- histone deacetylase inhibitors, isoform selectivity, histone acetylation, chromatin remodeling, tumor suppressor, apoptosis, tumor cell proliferation, inhibitor synthesis
- MeSH terms
- Animals, Histone Deacetylases, Humans, Models, Molecular, Zinc, Drug Discovery, Histone Deacetylase Inhibitors
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