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The Zinc-Binding Group Effect: Lessons from Non-Hydroxamic Acid Vorinostat Analogs
Open accessAbstract
Histone deacetylases (HDACs) are enzymes pursued as drug targets in various cancers and several non-oncological conditions, such as inflammation and neurodegenerative disorders. In the past decade, HDAC inhibitors (HDACi) have emerged as relevant pharmaceuticals, with many efforts devoted to the development of new representatives. However, the growing safety concerns regarding the established hydroxamic acid-based HDAC inhibitors tend to drive current research more toward the design of inhibitors bearing alternative zinc-binding groups (ZBGs). This Perspective presents an overview of all non-hydroxamic acid ZBGs that have been incorporated into the clinically approved prototypical HDACi, suberoylanilide hydroxamic acid (vorinostat). This provides the unique opportunity to compare the inhibition potential and biological effects of different ZBGs in a direct way, as the compounds selected for this Perspective differ only in their ZBG. To that end, different strategies used to select a ZBG, its properties, activity, and liabilities are discussed.
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“While most HDACi tend to employ a hydroxamic acid as a ZBG, class I HDACs (particularly HDACs 1–3) tend to be the only class of HDACs inhibited by 2-amino anilides as a ZBG (Figure 4A) [9–13].”
From Medicinal chemistry advances in targeting class I histone deacetylases (2023) · cites this paper as [13]
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“For this reason, RGFP966 (Figure 11) has emerged as the most frequently employed tool for HDAC3 pharmacologic inhibition in biological studies [9, 13, 67, 69–71].”
From Medicinal chemistry advances in targeting class I histone deacetylases (2023) · cites this paper as [13]
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Metadata
- Authors
- Geurs, S., Clarisse, D., De Bosscher, K., & D’hooghe, M.
- Affiliations
- Ghent University (BE)
- Translational Nuclear Receptor Research, VIB-UGent Center for Medical Biotechnology, Technologiepark-Zwijnaarde 75, B-9052 Ghent, Belgium
- Corresponding author
- D’hooghe, Matthias
- Venue
- Journal of Medicinal Chemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 2023-06-05
- Volume
- 66
- Issue
- 12
- Pages
- 7698-7729
- ISSN
- 0022-2623 (ISSN-L)
- 1520-4804
- OpenAlex
- W4379468009
- Cited by
- 58
- References
- 206
- Citations by year
- 2026: 20 · 2025: 19 · 2024: 14 · 2023: 5
- FWCI
- 1.53
- Type
- journal article
- Language
- en
- Open access
- green
- biblio.ugent.be
- Licence
- Locations
- Journal of Medicinal Chemistry (publishedVersion)
- PubMed (publishedVersion)
- Ghent University Academic Bibliography (Ghent University) (submittedVersion, other-oa)
- Funders
- Fonds Wetenschappelijk Onderzoek
- Bijzonder Onderzoeksfonds UGent
- 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
- Health Sciences › Medicine › Pharmacology (medical) › Cholinesterase and Neurodegenerative Diseases
- Keywords
- histone deacetylase inhibitors, vorinostat, zinc-binding groups, drug safety
- MeSH terms
- Vorinostat, Histone Deacetylases, Hydroxamic Acids, Zinc, Histone Deacetylase Inhibitors
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