ArticleAdvanced science (Weinheim, Baden-Wurttemberg, Germany)2024
Enzymolysis Modes Trigger Diversity in Inhibitor-α-Amylase Aggregating Behaviors and Activity Inhibition: A New Insight Into Enzyme Inhibition.
Article in Advanced science (Weinheim, Baden-Wurttemberg, Germany), 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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Who cites it
6 citing papers in PubMed.
- Versatile Microgel Platform for Intervertebral Disc Degeneration Therapy: Targeting Pericyte-Mediated Fibrosis and Protecting Nucleus Pulposus Cells.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Rapid and sensitive screening of carbonic anhydrase natural inhibitors in traditional Chinese medicine via a carbon quantum dot-affinity adsorption nanosystem.Journal of pharmaceutical analysis · 2026Article
- Comparative Study on the In Vitro Gastrointestinal Digestion of Oil Body Suspension from Different Parts ofGels (Basel, Switzerland) · 2026Article
- Interaction mechanisms in cassava starch-hemicellulose-sinapic acid ternary complex.Food chemistry: X · 2026Article
- Enzymolysis Modes Trigger Diversity in Inhibitor-α-Amylase Aggregating Behaviors and Activity Inhibition: A New Insight Into Enzyme Inhibition.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- Antidiabetic potential of a novel hydroxyphenyl-bi-benzopyran-hexol compound from Cassia fistula as an α-amylase inhibitor: Integrated in silico screening and in vitro validation using a nonlinear regression model.Journal of Ayurveda and integrative medicineArticle
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Authors and funding
7 authors.
Funding
Abstract
Inhibitors of α-amylase have been developed to regulate postprandial blood glucose fluctuation. The enzyme inhibition arises from direct or indirect inhibitor-enzyme interactions, depending on inhibitor structures. However, an ignored factor, substrate, may also influence or even decide the enzyme inhibition. In this work, it is innovatively found that the difference in substrate enzymolysis modes, i.e., structural composition and concentration of α-1,4-glucosidic bonds, triggers the diversity in inhibitor-enzyme aggregating behaviors and α-amylase inhibition. For competitive inhibition, there exists an equilibrium between α-amylase-substrate catalytic affinity and inhibitor-α-amylase binding affinity; therefore, a higher enzymolysis affinity and concentration of α-1,4-glucosidic structures interferes the balance, unfavoring inhibitor-enzyme aggregate formation and thus weakening α-amylase inhibition. For uncompetitive inhibition, the presence of macromolecular starch is necessary instead of micromolecular GalG2CNP, which not only binds with active site but with an assistant flexible loop (involving Gly
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Registered trials
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