{
  "abstract": "Psychotropic drugs are widely used to treat mental disorders, but they also influence cellular pathways linked to cancer. One key enzyme, Glutathione S-transferase (GST), is involved in detoxification and drug resistance in tumors, making it a potential target in cancer therapy. This study examined the effects of selected psychotropic agents aripiprazole, fluoxetine hydrochloride, risperidone, haloperidol, and sodium valproate on GST activity derived from equine liver. Enzyme kinetics were assessed in vitro using 1-chloro-2,4-dinitrobenzene (CDNB) as the substrate and ethacrynic acid (Kᵢ = 4.7 ± 0.8 nM) as the standard reference inhibitor. IC50 values were determined, and inhibition constants (Kᵢ) were calculated via Lineweaver-Burk plot analysis. The ranked Kᵢ values were as follows: Haloperidol (2.80 ± 1.6 nM) < Ethacrynic acid (4.70 ± 0.8 nM) < Risperidone (4.90 ± 0.39 nM) < Fluoxetine hydrochloride (5.40 ± 1.0 nM) < Aripiprazole (6.10 ± 0.7 nM) < Sodium valproate (386.0 ± 0.0 nM). Haloperidol showed the strongest GST inhibition among the tested drugs, even exceeding ethacrynic acid in binding affinity. This suggests its potential as a GST modulator in cancer therapy. Molecular docking studies revealed that the highest binding affinities were observed for Risperidone and Aripiprazole, showing scores of -7.350 to -7.576 Kcal/mol for 9GSS and -8.786 to -8.982 Kcal/mol for 5JCU. These strong interactions indicate a high potential of both compounds to effectively bind within the GST active site. The molecular dynamics simulation confirmed the stability and consistency of these complexes throughout the simulation period. Given the anticancer role of GST inhibitors, psychotropic drugs with significant GST inhibition especially haloperidol may positively contribute to cancer treatment.",
  "abstract_shown": true,
  "affiliations": [
    "Department of Psychiatry, Erzurum Faculty of Medicine, University of Health Sciences, Erzurum, Türkiye.",
    "Siran Dursun Keles Vocational School of Health Services, Gumushane University, Gümüshane, Türkiye.",
    "Department of Bioengineering, Architecture and Engineering Faculty, Kafkas University, Kars, Türkiye.",
    "Department of Basic Sciences, Faculty of Dentistry, Igdır University, Igdır, Türkiye.",
    "Department of Basic Medical Science, Medical of Faculty, Nakhchivan State University, Nakhchivan, Azerbaijan."
  ],
  "article_type": "research article",
  "arxiv": null,
  "author_total": 4,
  "authors": [
    {
      "affs": [
        0
      ],
      "name": "Elif Özcan Tozoğlu",
      "orcid": "0000-0003-2300-2634"
    },
    {
      "affs": [
        1
      ],
      "name": "Neslihan Balcı",
      "orcid": "0000-0002-1798-5550"
    },
    {
      "affs": [
        2
      ],
      "name": "Umit Yildiko",
      "orcid": "0000-0001-8627-9038"
    },
    {
      "affs": [
        3,
        4
      ],
      "name": "Fikret Türkan",
      "orcid": "0000-0002-0538-3157"
    }
  ],
  "bibtex": "https://research.draconitic.com/paper/10t0g5zwhgdxe.bib",
  "cited_by": 0,
  "doi": "10.1002/jbt.71165",
  "fulltext_url": "https://europepmc.org/articles/PMC13744385",
  "id": "10t0g5zwhgdxe",
  "issns": [
    "1095-6670",
    "1099-0461"
  ],
  "landing_url": "https://europepmc.org/article/MED/42998246",
  "language": "eng",
  "licence": "CC-BY-NC-ND",
  "licence_label": "CC BY-NC-ND",
  "licence_source": "article",
  "licence_url": "https://creativecommons.org/licenses/by-nc-nd/4.0/",
  "metadata_licence": null,
  "native_subjects": [
    [
      "openalex",
      "1312|Glutathione Transferases and Polymorphisms"
    ]
  ],
  "openalex": "W7225452747",
  "pdf_url": "https://europepmc.org/articles/PMC13744385?pdf=render",
  "pmcid": "PMC13744385",
  "pmid": "42998246",
  "published": "2026-11-01",
  "publisher": null,
  "ris": "https://research.draconitic.com/paper/10t0g5zwhgdxe.ris",
  "sources": [
    {
      "first_seen": "2026-11-09T15:20:34Z",
      "native_id": "MED:42998246",
      "source": "europepmc",
      "url": "https://europepmc.org/article/MED/42998246"
    }
  ],
  "subjects": [
    {
      "field": "biochemistry",
      "origin": "openalex:1312|Glutathione Transferases and Polymorphisms",
      "subfield": "molecular-biology"
    }
  ],
  "title": "Psychotropic Drug GST Interactions: In Vitro Inhibition, Molecular Docking, and Translational Potential in Cancer Therapy.",
  "title_text": "Psychotropic Drug GST Interactions: In Vitro Inhibition, Molecular Docking, and Translational Potential in Cancer Therapy.",
  "type": "peer-reviewed",
  "updated_at": "2026-11-09T15:20:34Z",
  "url": "https://research.draconitic.com/paper/10t0g5zwhgdxe",
  "venue": "Journal of biochemical and molecular toxicology",
  "versions": []
}