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RESEARCH PRODUCT

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

Fabrizio Lo CelsoGiosuè Lo BoscoClaudia MusialMagdalena Gorska-ponikowskaMagdalena Gorska-ponikowskaTomasz KostrzewaAlicja Kuban-jankowskaGiampaolo Barone

subject

0301 basic medicineAntioxidantPhysiologymedicine.medical_treatmentClinical BiochemistryPhosphataseProtein tyrosine phosphataseEpigallocatechin gallateBiochemistrycomplex mixturesArticle03 medical and health scienceschemistry.chemical_compound0302 clinical medicinebreast cancermedicineheterocyclic compoundsViability assayMolecular Biologyepigallocatechinprotein tyrosine phosphatase inhibitorChemistrylcsh:RM1-950food and beveragesPTP1BCell BiologyCatechin bindingIn vitro030104 developmental biologyEpicatechin gallatelcsh:Therapeutics. PharmacologyBiochemistrySettore CHIM/03 - Chimica Generale E Inorganica030220 oncology & carcinogenesissense organshormones hormone substitutes and hormone antagonistsgreen tea catechins

description

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.

10.3390/antiox9121208https://www.mdpi.com/2076-3921/9/12/1208