ArticleFoods (Basel, Switzerland)2026
Differential Inhibitory Mechanisms of Myricetin and Dihydromyricetin on α-Glucosidase: A Combined Molecular Docking, Isothermal Titration Calorimetry and Surface Plasmon Resonance Study.
Article in Foods (Basel, Switzerland), 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
α-Glucosidase inhibitors (AGIs) significantly regulate blood glucose by delaying carbohydrate digestion and slowing glucose absorption, thus playing a critical role in glycemic control. Structurally, dihydromyricetin (Unless otherwise stated, the term dihydromyricetin used throughout this manuscript refers to trans-(2R,3R)-(+)-dihydromyricetin.) differs from myricetin in that the C2=C3 double bond in the C-ring is saturated, resulting in a dihydroflavonol instead of a flavonol. This study investigated the inhibition mechanism of α-glucosidase by the C2=C3 double bond structure using a set of integrated and multi-perspective approaches combining enzyme kinetics, multi-spectroscopic methods, molecular docking, isothermal titration calorimetry (ITC), and surface plasmon resonance (SPR). Myricetin (IC
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