ArticleFrontiers in nutrition2021
Both Acidic pH Value and Binding Interactions of Tartaric Acid With α-Glucosidase Cause the Enzyme Inhibition: The Mechanism in α-Glucosidase Inhibition of Four Caffeic and Tartaric Acid Derivates.
Article in Frontiers in nutrition, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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7 citing papers in PubMed, 10 citations in OpenAlex.
- Bioactive Compounds and Antidiabetic Properties of Launaea mucronata Hydroethanolic Extract: Phytochemical and Pharmacological Insights.Chemistry & biodiversity · 2026Article
- Lactic acid bacteria fermentation improves the physicochemical properties, bioactivity, and metabolic profiles of lychee pulp.Food chemistry: X · 2026Article
- Inhibition mechanism and behaviour of wedelolactone against α-glucosidase.Journal of enzyme inhibition and medicinal chemistry · 2025Article
- Effect of Genistein on Starch Digestion In Vitro and Its Mechanism of Action.Foods (Basel, Switzerland) · 2024Article
- Naturally Occurring Functional Ingredient from Filamentous Thermophilic CyanobacteriumAntioxidants (Basel, Switzerland) · 2022Article
- Structural-Guided Identification of Small Molecule Inhibitor of UHRF1 Methyltransferase Activity.Frontiers in genetics · 2022Article
- α-Amylase Changed the Catalytic Behaviors of Amyloglucosidase Regarding Starch Digestion Both in the Absence and Presence of Tannic Acid.Frontiers in nutrition · 2022Article
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6 authors at 1 institution in 1 country.
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Abstract
The inhibition mechanism of four caffeic and tartaric acid derivates, including caffeic acid (CA), tartaric acid (TA), caftaric acid (CFA) and chicoric acid (CHA) against α-glucosidase was characterized by substrate depletion, fluorescence quenching, isothermal titration calorimetry (ITC) and molecular docking. TA and CA were found with the highest and no inhibition effect respectively, and caffeoyl substitution at 2 and/or 3-OH of TA significantly decreased its inhibition. The enzyme inhibition effects of organic acids were not in an inhibitor concentration-dependent mode, and there was a rush increase in inhibition at a respective acidic pH value, especially for CFA and CHA, suggesting the important role of acidic pH in the enzyme inhibition for both compounds. Besides, CA, CFA and CHA were shown with strong quenching effects on α-glucosidase fluorescence because of π-conjugations between aromatic ring of caffeoyl moiety and that of enzyme fluorescent residues. However, no fluorescence quenching effect was observed for TA due to lack of aromatic ring. Additionally, a direct binding interaction behavior was observed for TA with α-glucosidase according to the fitted independent binding model in ITC, but not for CFA and CHA. Therefore, both acidic pH and binding interactions of TA with α-glucosidase resulted in the enzyme inhibition.
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