In Vitro Inhibition of Glutathione-S-Transferase by Some Plant Extracts and Chemical Compounds

Abstract Glutathione-S-transferase (GST, EC 2.5.1.18) is a detoxification enzyme which belongs to the transferase enzyme family. This enzyme is found in many prokaryotic and all eukaryotic cells. GST catalyzes conjugation of reduced glutathione with exogen, mutagens, etc. The relation between increased GST activities and cancer cases have directed researchers to investigate the possible inhibition of this enzyme. For this reason, phytochemicals are at the center of this research due to their useful properties. In this study, we aimed to investigate the potentials of plant extracts and chemical compounds to inhibit GST. GST inhibitory effects of various samples were determined according to Habig et al. method. The inhibition assays were determined spectrophotometrically at 340 nm as considering absorbance alteration between zero and third minutes. 1‑Chloro-2,4-dinitro benzene was used as substrate. In our study, aqueous plant extracts were prepared. Among the plant extracts, chard (IC50 = 17.01 ± 1.16 mg/mL), spinach (IC50 = 24.93 ± 2.86 mg/mL), and lemon (IC50 = 29.32 ± 2.98 mg/mL) showed the best inhibition. Among the chemical substances, bivalent compounds of copper (IC50 = 5.72 ± 0.13 mM), cadmium (IC50 = 5.86 ± 0.55 mM), zinc (IC50 = 25.68 ± 1.62 mM), and vitamin B6 (IC50 = 16.26 ± 2.72 mM) were observed as the best inhibitory chemical compounds. When we consider the phytochemical screening of plant extracts and the structures of chemical compounds, we can hypothesize that they could be new targets in cancer treatments as targets for GST inhibition.

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Publication Details

Journal
Moscow University Chemistry Bulletin
Published
2026-09-09
DOI
https://doi.org/10.3103/s0027131426700264
Primary Topic
Glutathione Transferases and Polymorphisms
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article
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article

In Vitro Inhibition of Glutathione-S-Transferase by Some Plant Extracts and Chemical Compounds

İsmet Burcu Türkyılmaz, Refiye Yanardağ, Cemre Babaoglu
Moscow University Chemistry Bulletin
Glutathione Transferases and Polymorphisms
article

In Vitro Inhibition of Glutathione-S-Transferase by Some Plant Extracts and Chemical Compounds

İsmet Burcu Türkyılmaz, Refiye Yanardağ, Cemre Babaoglu
article en

Abstract

Abstract Glutathione-S-transferase (GST, EC 2.5.1.18) is a detoxification enzyme which belongs to the transferase enzyme family. This enzyme is found in many prokaryotic and all eukaryotic cells. GST catalyzes conjugation of reduced glutathione with exogen, mutagens, etc. The relation between increased GST activities and cancer cases have directed researchers to investigate the possible inhibition of this enzyme. For this reason, phytochemicals are at the center of this research due to their useful properties. In this study, we aimed to investigate the potentials of plant extracts and chemical compounds to inhibit GST. GST inhibitory effects of various samples were determined according to Habig et al. method. The inhibition assays were determined spectrophotometrically at 340 nm as considering absorbance alteration between zero and third minutes. 1‑Chloro-2,4-dinitro benzene was used as substrate. In our study, aqueous plant extracts were prepared. Among the plant extracts, chard (IC50 = 17.01 ± 1.16 mg/mL), spinach (IC50 = 24.93 ± 2.86 mg/mL), and lemon (IC50 = 29.32 ± 2.98 mg/mL) showed the best inhibition. Among the chemical substances, bivalent compounds of copper (IC50 = 5.72 ± 0.13 mM), cadmium (IC50 = 5.86 ± 0.55 mM), zinc (IC50 = 25.68 ± 1.62 mM), and vitamin B6 (IC50 = 16.26 ± 2.72 mM) were observed as the best inhibitory chemical compounds. When we consider the phytochemical screening of plant extracts and the structures of chemical compounds, we can hypothesize that they could be new targets in cancer treatments as targets for GST inhibition.

Moscow University Chemistry BulletinVol. 81(5)
Istanbul University-Cerrahpaşa (TR), Istanbul University (TR)
Openalex Percentile: Top 17%
Glutathione Transferases and Polymorphisms
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