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Green Tea Catechins Induce Inhibition of PTP1B Phosphatase in Breast Cancer Cells with Potent Anti-Cancer Properties: In Vitro Assay, Molecular Docking, and Dynamics Studies.
Kuban-Jankowska, Alicja; Kostrzewa, Tomasz; Musial, Claudia; Barone, Giampaolo; Lo Bosco, Giosuè; Lo Celso, Fabrizio; Gorska-Ponikowska, Magdalena.
  • Kuban-Jankowska A; Medical Chemistry Department, Medical University of Gdansk, 80-210 Gdansk, Poland.
  • Kostrzewa T; Medical Chemistry Department, Medical University of Gdansk, 80-210 Gdansk, Poland.
  • Musial C; Medical Chemistry Department, Medical University of Gdansk, 80-210 Gdansk, Poland.
  • Barone G; Department of Biological, Chemical and Pharmaceutical Sciences and Technologies, University of Palermo, 90128 Palermo, Italy.
  • Lo Bosco G; Department of Mathematics and Computer Science, University of Palermo, 90133 Palermo, Italy.
  • Lo Celso F; The Euro-Mediterranean Institute of Science and Technology, 90139 Palermo, Italy.
  • Gorska-Ponikowska M; Department of Physics and Chemistry 'Emilio Segrè', University of Palermo, 90128 Palermo, Italy.
Antioxidants (Basel) ; 9(12)2020 Nov 30.
Article en En | MEDLINE | ID: mdl-33266280
The catechins derived from green tea possess antioxidant activity and may have a potentially anticancer effect. PTP1B is tyrosine phosphatase that is oxidative stress regulated and is involved with prooncogenic pathways leading to the formation of a.o. breast cancer. Here, we present the effect of selected green tea catechins on enzymatic activity of PTP1B phosphatase and viability of MCF-7 breast cancer cells. We showed also the computational analysis of the most effective catechin binding with a PTP1B molecule. We observed that epigallocatechin, epigallocatechin gallate, epicatechin, and epicatechin gallate may decrease enzymatic activity of PTP1B phosphatase and viability of MCF-7 cells. Conclusions: From the tested compounds, epigallocatechin and epigallocatechin gallate were the most effective inhibitors of the MCF-7 cell viability. Moreover, epigallocatechin was also the strongest inhibitor of PTP1B activity. Computational analysis allows us also to conclude that epigallocatechin is able to interact and bind to PTP1B. Our results suggest also the most predicted binding site to epigallocatechin binding to PTP1B.
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