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Purpose <p>Diabetes mellitus is a global health challenge, and effective and affordable therapies are crucial. Myricetin is a naturally occurring flavonoid, has demonstrated promising antidiabetic potential. The current research aims to investigate the binding affinity and molecular interactions of myricetin with alpha-amylase and 1OSE protein, and to explore its potential as a therapeutic agent for diabetes management.</p> Methods <p>The present study is associated with the molecular docking of myricetin against diabetes linked targets, which was investigated through Auto Dock Vina, PyRx, and Schrodinger Glide. The protein structures were prepared by eliminating water molecules and any co-crystallized ligands. The 3D structures of target proteins, including 1OSE, as well as α-amylase, were retrieved from the Protein Data Bank (PDB). The therapeutic targets were prepared in PDBQT format. The chemical structure of myricetin was obtained from the PubChem database. The ligand structure was stabilized to achieve a stable conformation and converted into PDBQT format using PyRx and Open Babel. AutoDock Vina integrated within PyRx software, was used for molecular docking used for computational effectiveness. The best docking poses were selected based on binding energy scores and interaction profiles. Bond distances, protein–ligand interactions, including hydrogen bonding, hydrophobic interactions, were visualized as well as analysed using molecular visualization tools such as PyMOL and Discovery Studio. In vitro alpha amylase assay preformed and IC₅₀ values were determined. Statistical analysis performed to know significance between treatment groups.</p> Results <p>Myricetin exhibited a strong and stable binding affinity toward alpha-amylase and 1OSE protein, with a binding energy of -8.8 to -7.6 kcal/mol indicating stable interactions within the active site.</p> Conclusion <p>Myricetin exhibits promise as a therapeutic agent for diabetes mitigation owing to its strong binding affinity and inhibitory activity against alpha-amylase.</p>

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Alpha-amylase Inhibition by Myricetin Nanoparticles: An In Silico, In Vitro, and In Vivo Evaluation toward Natural Antidiabetic Therapy

  • 期刊论文

  • 发表日期：

    2026年5月9日

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  • Karishma Ramchandra Waghmare,
  • Guno Sindhu Chakraborthy

摘要

Purpose

Diabetes mellitus is a global health challenge, and effective and affordable therapies are crucial. Myricetin is a naturally occurring flavonoid, has demonstrated promising antidiabetic potential. The current research aims to investigate the binding affinity and molecular interactions of myricetin with alpha-amylase and 1OSE protein, and to explore its potential as a therapeutic agent for diabetes management.

Methods

The present study is associated with the molecular docking of myricetin against diabetes linked targets, which was investigated through Auto Dock Vina, PyRx, and Schrodinger Glide. The protein structures were prepared by eliminating water molecules and any co-crystallized ligands. The 3D structures of target proteins, including 1OSE, as well as α-amylase, were retrieved from the Protein Data Bank (PDB). The therapeutic targets were prepared in PDBQT format. The chemical structure of myricetin was obtained from the PubChem database. The ligand structure was stabilized to achieve a stable conformation and converted into PDBQT format using PyRx and Open Babel. AutoDock Vina integrated within PyRx software, was used for molecular docking used for computational effectiveness. The best docking poses were selected based on binding energy scores and interaction profiles. Bond distances, protein–ligand interactions, including hydrogen bonding, hydrophobic interactions, were visualized as well as analysed using molecular visualization tools such as PyMOL and Discovery Studio. In vitro alpha amylase assay preformed and IC₅₀ values were determined. Statistical analysis performed to know significance between treatment groups.

Results

Myricetin exhibited a strong and stable binding affinity toward alpha-amylase and 1OSE protein, with a binding energy of -8.8 to -7.6 kcal/mol indicating stable interactions within the active site.

Conclusion

Myricetin exhibits promise as a therapeutic agent for diabetes mitigation owing to its strong binding affinity and inhibitory activity against alpha-amylase.