ArticleFoods (Basel, Switzerland)2024
Exploring the Blood Glucose-Lowering Potential of the Umami Peptides LADW and EEAEGT Derived from Tuna Skeletal Myosin: Perspectives from α-Glucosidase Inhibition and Starch Interaction.
Article in Foods (Basel, Switzerland), 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 21 citations in OpenAlex.
- Article
- Peptidomics-guided 3D structural-mechanistic investigation of bovine colostrum peptides reveals multi-targetedFood chemistry: X · 2026Article
- In Vitro Antioxidant Activity and Dual-Target Inhibitory Effects of Dipyridamole on α-Amylase and α-Glucosidase: Molecular Mechanisms and Molecular Dynamics Simulations.Biomolecules · 2026Article
- Food-Derived Antidiabetic Peptides as Multi-Target Systemic Regulators: A Comprehensive Review of Sources, Preparation, Mechanisms and Future Perspectives.Foods (Basel, Switzerland) · 2026Review
- Identification, Molecular Docking Mechanism and Cellular Activity of Selenium-Enriched ACE Inhibitory Peptides from Oysters.Molecules (Basel, Switzerland) · 2025Article
- Article
- Comparative study of the effects of different lipid oxidation simulation systems on the physicochemical properties of proteins isolated from four cultivated walnut (Food chemistry: X · 2025Article
- Investigating the inflammatory mechanism of notoginsenoside R1 in Diabetic nephropathy via ITGB8 based on network pharmacology and experimental validation.Molecular medicine (Cambridge, Mass.) · 2024Article
- Article
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
This study aimed to explore the potential of umami peptides for lowering blood glucose. Molecular docking results showed that the peptides LADW and EEAEGT bound to the active amino acid residues of α-glucosidase via hydrogen bonds and Van der Waals forces, a finding supported by an independent gradient model (IGM). Molecular dynamics (MD) simulations demonstrated that the peptides LADW and EEAEGT can decelerate the outward expansion of α-glucosidase and reduce amino acid fluctuations at the active site. In vitro findings indicated that the peptides LADW and EEAEGT showed potent inhibitory activity against α-glucosidase, with IC
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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 Socratic graph.