Related Experiment Video
Updated: Sep 14, 2025

Author Spotlight: Integrating Biochemical Functions of β-Glucanases and Peroxidase Enzymes in Wheat-RWA Interaction
Published on: July 26, 2024
Mechanistic insight into the inhibition of α-glucosidase by millet Prolamin K3ZAN2: An integrated experimental and
Liangxing Zhao1,2,3, Ruikang Lin1,2,3, Xinlai Dou1,2,3
1College of Food Science and Nutritional Engineering, China Agricultural University, Beijing 100083, China.
Abstract:
Dietary proteins with α-glucosidase inhibitory activity are gaining interest for their role in supporting glycemic control. Here, we report that millet-derived prolamin K3ZAN2 modulates α-glucosidase activity through a flexible-region-mediated mechanism. K3ZAN2 exhibited an IC₅₀ of 4.15 mg/mL, with its proteinaceous nature confirmed by UV spectroscopy and SDS-PAGE. Molecular docking showed that flexible residues Thr11, Ser18, Gln20, Gly26, and Gln64 interact with α-glucosidase active site residues via hydrogen bonds and hydrophobic interactions. Molecular dynamics simulations (102 ns) indicated structural stability (RMSD ∼0.2 nm), compactness (Rg ∼1.9 nm), and persistent hydrogen bonding. Binding free energy (ΔG = -15,536.71 kJ/mol) supported strong affinity. Principal component and free energy landscape analyses revealed conformational transitions and stable states, while dynamic cross-correlation analysis highlighted coordinated motions at the interface. These computational insights support a dynamic binding model, enhancing the understanding of food protein-enzyme interactions relevant to glycemic regulation.
More Related Videos
Related Concept Videos
Oral Hypoglycemic Agents: α-Glucosidase Inhibitors
Acarbose and miglitol are...
Dipeptidyl Peptidase 4 Inhibitors
Enzyme Inhibition
Glucagon-like Receptor Agonists
GLP-1, when administered in high doses intravenously, triggers insulin secretion, inhibits glucagon release, slows gastric emptying, reduces food intake, and restores normal insulin secretion. However, its rapid inactivation by...

