ArticleBiomolecules2022
Myricetin as a Potential Adjuvant in Chemotherapy: Studies on the Inhibition of Human Glutathione Transferase A1-1.
Article in Biomolecules, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 14 citations in OpenAlex.
- Potential dietary geroprotectors and their impact on key mechanisms of aging.Biogerontology · 2025Review
- Modulation of Glutathione-S-Transferase by Phytochemicals: To Activate or Inhibit-That Is the Question.International journal of molecular sciences · 2025Review
- Article
- Organic Sunscreens-Is Their Placenta Permeability the Only Issue Associated with Exposure During Pregnancy? In Silico Studies of Sunscreens' Placenta Permeability and Interactions with Selected Placental Enzymes.Molecules (Basel, Switzerland) · 2024Article
- MiR-133 promotes the multidrug resistance of acute myeloid leukemia cells (HL-60/ADR) to daunorubicin.Cytotechnology · 2024Article
- A Monocarbonyl Curcuminoid Derivative Inhibits the Activity of Human Glutathione Transferase A4-4 and Chemosensitizes Glioblastoma Cells to Temozolomide.Pharmaceuticals (Basel, Switzerland) · 2024Article
- Novel coumarin-6-sulfonamide-chalcone hybrids as glutathione transferase P1-1 inhibitors.PloS one · 2024Article
- Overexpression of Glutathione S-Transferases in Human Diseases: Drug Targets and Therapeutic Implications.Antioxidants (Basel, Switzerland) · 2023Review
- Recent studies on myricetin and its biological and pharmacological activities.EXCLI journal · 2023Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Glutathione transferases (GSTs) are a family of Phase II detoxification enzymes that are involved in the development of multi-drug resistance (MDR) phenomena toward chemotherapeutic agents. GST inhibitors are considered candidate compounds able to chemomodulate and reverse MDR. The natural flavonoid myricetin (MYR) has been shown to exhibit a wide range of pharmacological functions, including antitumor activity. In the present work, the interaction of MYR with human glutathione transferase A1-1 (hGSTA1-1) was investigated by kinetics inhibition analysis and molecular modeling studies. The results showed that MYR binds with high affinity to hGSTA1-1 (IC50 2.1 ± 0.2 μΜ). It functions as a non-competitive inhibitor towards the electrophile substrate 1-chloro-2,4-dinitrobenzene (CDNB) and as a competitive inhibitor towards glutathione (GSH). Chemical modification studies with the irreversible inhibitor phenethyl isothiocyanate (PEITC), in combination with in silico molecular docking studies allowed the prediction of the MYR binding site. MYR appears to bind at a distinct location, partially overlapping the GSH binding site (G-site). The results of the present study show that MYR is a potent inhibitor of hGSTA1-1 that can be further exploited towards the development of natural, safe, and effective GST-targeted cancer chemosensitizers.
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