ArticlePloS one2014
Inhibition of catalase by tea catechins in free and cellular state: a biophysical approach.
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 58 citations in OpenAlex.
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- Experimental and Theoretical Approaches to Monitor the Behavior of Bovine Liver Catalase in Interaction with a Binuclear Bismuth Complex.ACS omega · 2024Article
- Catalases in the pathogenesis ofPeerJ · 2022Review
- Systems Network Pharmacology-Based Prediction and Analysis of Potential Targets and Pharmacological Mechanism ofEvidence-based complementary and alternative medicine : eCAM · 2022Article
- Article
- Iron Complexes of Flavonoids-Antioxidant Capacity and Beyond.International journal of molecular sciences · 2021Review
- Epigallocatechin-3-Gallate Promotes the in vitro Maturation and Embryo Development Following IVF of Porcine Oocytes.Drug design, development and therapy · 2021Article
- Solid Lipid Microparticles for Oral Delivery of Catalase: Focus on the Protein Structural Integrity and Gastric Protection.Molecular pharmaceutics · 2020Article
- Interaction of Catechins with Human Erythrocytes.Molecules (Basel, Switzerland) · 2020Article
- Preclinical Pharmacological Activities of Epigallocatechin-3-gallate in Signaling Pathways: An Update on Cancer.Molecules (Basel, Switzerland) · 2020Review
- Physicochemical characterization of dual action liposomal formulations: anticancer and antimicrobial.Heliyon · 2019Article
- In Vitro and In Silico Studies of the Molecular Interactions of Epigallocatechin-3-Molecules (Basel, Switzerland) · 2018Review
- Development of an assay to assess genotoxicity by particulate matter extract.Molecular medicine reports · 2017Article
- Characterization of Active Anthocyanin Degradation in the Petals of Rosa chinensis and Brunfelsia calycina Reveals the Effect of Gallated Catechins on Pigment Maintenance.International journal of molecular sciences · 2017Article
- Inhibition of cancer antioxidant defense by natural compounds.Oncotarget · 2017Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Tea flavonoids bind to variety of enzymes and inhibit their activities. In the present study, binding and inhibition of catalase activity by catechins with respect to their structure-affinity relationship has been elucidated. Fluorimetrically determined binding constants for (-)-epigallocatechin gallate (EGCG) and (-)-epicatechin gallate (ECG) with catalase were observed to be 2.27×106 M(-1) and 1.66×106 M(-1), respectively. Thermodynamic parameters evidence exothermic and spontaneous interaction between catechins and catalase. Major forces of interaction are suggested to be through hydrogen bonding along with electrostatic contributions and conformational changes. Distinct loss of α-helical structure of catalase by interaction with EGCG was captured in circular dichroism (CD) spectra. Gallated catechins demonstrated higher binding constants and inhibition efficacy than non-gallated catechins. EGCG exhibited maximum inhibition of pure catalase. It also inhibited cellular catalase in K562 cancer cells with significant increase in cellular ROS and suppression of cell viability (IC50 54.5 µM). These results decipher the molecular mechanism by which tea catechins interact with catalase and highlight the potential of gallated catechin like EGCG as an anticancer drug. EGCG may have other non-specific targets in the cell, but its anticancer property is mainly defined by ROS accumulation due to catalase inhibition.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.