ArticleJournal of molecular modeling2018
Hydroxamic acid derivatives as histone deacetylase inhibitors: a DFT study of their tautomerism and metal affinities/selectivities.
Article in Journal of molecular modeling, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 10 citations in OpenAlex.
- Zinc Affinity of Benzamide-Based Histone Deacetylase Inhibitors: A DFT Study.Molecules (Basel, Switzerland) · 2026Article
- Metal Preference Hierarchy in the HDAC8 Active Site: A DFT Study.Molecules (Basel, Switzerland) · 2026Article
- Synthesis and HDAC inhibitory activity of pyrimidine-based hydroxamic acids.Beilstein journal of organic chemistry · 2022Article
- The Effect of Organoselenium Compounds on Histone Deacetylase Inhibition and Their Potential for Cancer Therapy.International journal of molecular sciences · 2021Review
- Screening of an Epigenetic Drug Library Identifies 4-((hydroxyamino)carbonyl)-International journal of molecular sciences · 2020Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Hydroxamic acids are regarded as potent inhibitors of histone deacetylases (HDAC), and can therefore be used to reduce malignancy growth and size in affected organisms. Although there is a substantial body of information on the structures, syntheses, and biological activities of HDAC inhibitors, several important questions regarding their physicochemical properties and metal affinities/selectivities remain answered. First, how do the conformation and ionization of the hydroxamic group depend on its chemical composition and the dielectric properties of the medium? Second, how do these factors affect the affinities and selectivities of HDAC inhibitors for essential biogenic metal cations? Third, what is the preferred deprotonation site of the hydroxamic moiety and its mode of binding to the metal cation? The present work addressed these questions by performing density functional calculations combined with polarizable continuum model computations. The geometry, deprotonation pattern, metal-binding mode, and metal affinity/selectivity of SAHA, a typical HDAC inhibitor, were examined, and key factors affecting its ligation properties were elucidated. Sulfur- and selenium-containing analogs of SAHA were also modeled for the first time, and their potential as efficient metal-binding entities (to Mg
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