ArticleFrontiers in nutrition2022
Structural changes and molecular mechanism study on the inhibitory activity of epigallocatechin against α-glucosidase and α-amylase.
Article in Frontiers in nutrition, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
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Who cites it
11 citing papers in PubMed, 18 citations in OpenAlex.
- Development of Epigallocatechin-Loaded Water Caltrop Starch Aerogels: Structure, Functional Properties and In Vitro Release Behavior.Foods (Basel, Switzerland) · 2026Article
- In Vitro Antidiabetic Activity of Phenolic Compounds from NADES-Extracted SunGold Kiwifruit and Their Fortification in Yoghurt.Foods (Basel, Switzerland) · 2026Article
- In Vitro Inhibition of Digestive Enzymes by Leaf Metabolites fromMolecules (Basel, Switzerland) · 2026Article
- Review
- Bioactivity-Guided Identification of Metabolites fromMolecules (Basel, Switzerland) · 2026Article
- Preparation and Mechanistic Characterization of α-Glucosidase Inhibitory Peptides fromFoods (Basel, Switzerland) · 2026Article
- Dietary Green Tea Enhances the Growth, Antioxidant Capacity, and Abundance of Beneficial Intestinal Flora of Grass Carp (Animals : an open access journal from MDPI · 2025Article
- Integrated computational and experimental evaluation of grossamide as a natural product scaffold for dual carbohydrase inhibition in diabetes.Journal of computer-aided molecular design · 2025Article
- Eco-friendly synthesis of silver nanoparticles: multifaceted antioxidant, antidiabetic, anticancer, and antimicrobial activities.Scientific reports · 2025Article
- Avocado (Frontiers in nutrition · 2025Review
- α-Glucosidase inhibitory activity of polyphenol-rich sugarcane extract: screening and mechanistic insights based on biolayer interferometry-mass spectrometry.Frontiers in nutrition · 2025Article
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
In this study, the inhibition and mechanism of epigallocatechin (EGC) on two key glycoside hydrolases (α-glucosidase, α-amylase) were explored from the molecular structure level. The chemical structure of EGC was characterized by X-ray diffraction, Fourier transform infrared (FTIR) spectroscopy, and proton nuclear magnetic resonance spectroscopy. EGC's inhibition on these enzymes was colorimetrically determined. The effects of EGC on the chemical structure and spatial configuration of the enzymes were explored
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Registered trials
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