ArticlePloS one2012
Influence of galloyl moiety in interaction of epicatechin with bovine serum albumin: a spectroscopic and thermodynamic characterization.
Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 48 citations in OpenAlex.
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- Combination Therapy for Sustainable Fish Oil Products: Improving Cognitive Function with n-3 PUFA and Natural Ingredients.Biomedicines · 2024Review
- Molecular characterization ofSaudi journal of biological sciences · 2021Article
- Modulation of DNA structure formation using small molecules.Biochimica et biophysica acta. Molecular cell research · 2019Review
- Visible-Light-Activated Quinolone Carbon-Monoxide-Releasing Molecule: Prodrug and Albumin-Assisted Delivery Enables Anticancer and Potent Anti-Inflammatory Effects.Journal of the American Chemical Society · 2018Article
- Thermodynamic and computational analyses reveal the functional roles of the galloyl group of tea catechins in molecular recognition.PloS one · 2018Article
- Characterization of molecular structures of theaflavins and the interactions with bovine serum albumin.Journal of food science and technology · 2017Article
- N- and S-homocysteinylation reduce the binding of human serum albumin to catechins.European journal of nutrition · 2017Article
- Human Serum Albumin Increases the Stability of Green Tea Catechins in Aqueous Physiological Conditions.PloS one · 2015Article
- Salivary α-amylase, serum albumin, and myoglobin protect against DNA-damaging activities of ingested dietary agents in vitro.Food and chemical toxicology : an international journal published for the British Industrial Biological Research Association · 2014Article
- Inhibition of catalase by tea catechins in free and cellular state: a biophysical approach.PloS one · 2014Article
- Factors influencing the antifolate activity of synthetic tea-derived catechins.Molecules (Basel, Switzerland) · 2013Article
- Epicatechin-induced conformational changes in β-lactoglobulin B monitored by FT-IR spectroscopy.SpringerPlus · 2013Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The health benefits stemming from green tea are well known, but the exact mechanism of its biological activity is not elucidated. Epicatechin (EC) and epicatechin gallate (ECG) are two dietary catechins ubiquitously present in green tea. Serum albumins functionally carry these catechins through the circulatory system and eliminate reactive oxygen species (ROS) induced injury. In the present study ECG is observed to have higher antioxidant activity; which is attributed to the presence of galloyl moiety. The binding affinity of these catechins to bovine serum albumin (BSA) will govern the efficacy of their biological activity. EC and ECG bind with BSA with binding constants 1.0 × 10(6) M(-1) and 6.6 × 10(7) M(-1), respectively. Changes in secondary structure of BSA on interaction with EC and ECG have been identified by circular dichroism (CD) and Fourier transform infrared (FT-IR) spectroscopy. Thermodynamic characterization reveals the binding process to be exothermic, spontaneous and entropy driven. Mixed binding forces (hydrophobic, electrostatic and hydrogen bonding) exist between ECG and BSA. Binding site for EC is primarily site-II in sub-domain IIIA of BSA and for ECG; it is site-I in sub-domain IIA. ECG with its high antioxidant activity accompanied by high affinity for BSA could be a model in drug designing.
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