ArticlePloS one2014
Molecular interactions between (-)-epigallocatechin gallate analogs and pancreatic lipase.
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 19 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
19 citing papers in PubMed, 54 citations in OpenAlex.
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- The In Vitro Inhibitory Effect of Selected Asteraceae Plants on Pancreatic Lipase Followed by Phenolic Content Identification through Liquid Chromatography High Resolution Mass Spectrometry (LC-HRMS).International journal of molecular sciences · 2022Article
- 4″-Sulfation Is the Major Metabolic Pathway of Epigallocatechin-3-gallate in Humans: Characterization of Metabolites, Enzymatic Analysis, and Pharmacokinetic Profiling.Journal of agricultural and food chemistry · 2022Article
- Polyphenols andJournal of preventive medicine and hygiene · 2022Review
- Catechins as a Potential Dietary Supplementation in Prevention of Comorbidities Linked with Down Syndrome.Nutrients · 2022Review
- ( -)-Epicatechin and cardiometabolic risk factors: a focus on potential mechanisms of action.Pflugers Archiv : European journal of physiology · 2022Review
- Targeting Carbohydrates and Polyphenols for a Healthy Microbiome and Healthy Weight.Current nutrition reports · 2019Review
- Inhibition of CpLIP2 Lipase Hydrolytic Activity by Four Flavonols (Galangin, Kaempferol, Quercetin, Myricetin) Compared to Orlistat and Their Binding Mechanisms Studied by Quenching of Fluorescence.Molecules (Basel, Switzerland) · 2019Article
- Computational Molecular Docking and X-ray Crystallographic Studies of Catechins in New Drug Design Strategies.Molecules (Basel, Switzerland) · 2018Review
- In Vitro and In Silico Studies of the Molecular Interactions of Epigallocatechin-3-Molecules (Basel, Switzerland) · 2018Review
- A Review on the Weight-Loss Effects of Oxidized Tea Polyphenols.Molecules (Basel, Switzerland) · 2018Review
- Thermodynamic and computational analyses reveal the functional roles of the galloyl group of tea catechins in molecular recognition.PloS one · 2018Article
- The Role of Polyphenols in Human Health and Food Systems: A Mini-Review.Frontiers in nutrition · 2018Review
- Antioxidants from black and green tea: from dietary modulation of oxidative stress to pharmacological mechanisms.British journal of pharmacology · 2017Review
- Polyphenolic Compounds and Digestive Enzymes: In Vitro Non-Covalent Interactions.Molecules (Basel, Switzerland) · 2017Review
- Inhibition of pancreatic lipase by black tea theaflavins: Comparative enzymology and in silico modeling studies.Food chemistry · 2017Article
- Epigallocatechin Gallate: A Review of Its Beneficial Properties to Prevent Metabolic Syndrome.Nutrients · 2015Review
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The molecular interactions between pancreatic lipase (PL) and four tea polyphenols (EGCG analogs), like (-)-epigallocatechin gallate (EGCG), (-)-gallocatechin gallate (GCG), (-)-epicatechin gallate (ECG), and (-)-epigallocatechin (EC), were studied from PL activity, conformation, kinetics and thermodynamics. It was observed that EGCG analogs inhibited PL activity, and their inhibitory rates decreased by the order of EGCG>GCG>ECG>EC. PL activity at first decreased rapidly and then slowly with the increase of EGCG analogs concentrations. α-Helix content of PL secondary structure decreased dependent on EGCG analogs concentration by the order of EGCG>GCG>ECG>EC. EGCG, ECG, and EC could quench PL fluorescence both dynamically and statically, while GCG only quenched statically. EGCG analogs would induce PL self-assembly into complexes and the hydrodynamic radii of the complexes possessed a close relationship with the inhibitory rates. Kinetics analysis showed that EGCG analogs non-competitively inhibited PL activity and did not bind to PL catalytic site. DSC measurement revealed that EGCG analogs decreased the transition midpoint temperature of PL enzyme, suggesting that these compounds reduced PL enzyme thermostability. In vitro renaturation through urea solution indicated that interactions between PL and EGCG analogs were weak and non-covalent.
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Registered trials
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.