A new α-amylase inhibitory peptide from Gynura medica extract.

Food Chem

School of Food and Biological Engineering, Key Laboratory of Industrial Biotechnology in Tobacco Industry, Zhengzhou University of Light Industry, 136 Kexuedadao Road, 450008 Zhengzhou, China. Electronic address:

Published: April 2024

In this study, we discovered a novel peptide, Gymepeptide A, with α-amylase inhibitory activity in the water extract of Gynura medica. The structure of Gymepeptide A was determined as CGDREETR using HR-MS, H NMR, C NMR, and 2D-NMR techniques. Notably, Gymepeptide A possesses a rare double arginine residue structure and exhibits strong α-amylase inhibitory activity. Enzyme dynamic assays, molecular docking experiments, and isothermal titration calorimetry indicated that the double arginine residue structure of Gymepeptide A interacts with amino acid residues in the nearby active site region of α-amylase through hydrogen bonds and van der Waals forces. This interaction effectively inhibits the hydrolysis activity of α-amylase. Furthermore, in vitro starch digestion tests revealed that Gymepeptide A significantly reduced the digestion rate of starch and the concentration of glucose produced after starch digestion. These findings highlight the great potential of Gymepeptide A in decreasing postprandial blood glucose levels.

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http://dx.doi.org/10.1016/j.foodchem.2023.137959DOI Listing

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