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Histone Deacetylase Inhibitors Research · Journal article
European Journal of Biology · September 7, 2026
Raises a question worth testing. It does not answer one.
This is a screen of organosulfur compounds for in vitro inhibition of three cancer-related enzymes (HDAC, carbonic anhydrase, xanthine oxidase) using biochemical assays. While several compounds showed measurable IC₅₀ values, the work is preclinical and exploratory; it does not establish mechanism of anticancer action, cellular efficacy, or advancement toward drug development.
In vitro biochemical screening study. Intervention: Organosulfur compounds including L-cysteine hydrochloride, L-alliin, D,L-methionine, N-acetyl-L-cysteine, S-allyl-L-cysteine, S-phenyl-L-cysteine, and S-benzyl-L-cysteine.
L-alliin showed lowest IC₅₀ for XO inhibition at 0.0000419 mg/mL L-cysteine hydrochloride had lowest IC₅₀ for HDAC inhibition at 17.66 mg/mL D,L-methionine and N-acetyl-L-cysteine inhibited HDAC with IC₅₀ values of 18.76 mg/mL and 29.02 mg/mL respectively
Safety was not reported in the material analysed. Check the source before drawing any conclusion about harm.
The source did not state who this applies to in practice.
In vitro enzyme inhibition study of organosulfur compounds against three targets; no cellular, animal, or clinical validation reported, and no comparison to established drugs or positive controls.
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Objective: Histone deacetylases (HDACs) are critical epigenetic regulators of gene expression and represent important pharmacological targets in cancer therapy. Moreover, carbonic anhydrase (CA) and xanthine oxidase (XO) are key enzymes involved in cellular homeostasis, including pH regulation, ion transport, oxygen metabolism, and oxidative stress, all of which are closely associated with tumour progression and cancer-related metabolic reprogramming. Considering the pharmacological relevance of these enzymes, organosulphur compounds—known for their antioxidant, anti inflammatory, immunomodulatory, antimicrobial, and antiaging properties—were evaluated for their anticancer-related enzyme inhibitory activity against HDAC, CA, and XO.Materials and Methods: Fluorometric and spectrophotometric assays were used to evaluate the anti-HDAC, anti-CA, and anti-XO activities of the sulphur compounds.Results: L-cysteine hydrochloride (IC50=17. 66 mg/mL) and L-alliin (IC50=0.0000419 mg/mL) had the lowest IC50 value for HDAC and XO inhibitor activities among the sulphur compounds, respectively. D,L-methionine (IC50=18.76 mg/mL) and N-acetyl-L-cysteine (IC50=29.02 mg/mL) inhibited HDAC activity more than the other tested compounds. All tested organosulphur compounds, such as N-acetyl-L-cysteine, L-cysteine hydrochloride, S-allyl-L-cysteine, S-phenyl-L-cysteine, and S-benzyl-L-cysteine, exhibited CA inhibitory activities.Conclusion: These organosulphur compounds exhibited in vitro inhibitory activity against cancer-related target enzymes and may serve as promising lead compounds for further anticancer research.
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