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Screening and Activity Analysis of α-Glucosidase Inhibitory Peptides Derived from Coix Seed Prolamins Using Bioinformatics and Molecular Docking

Hydrolysates of coix seed prolamins (CHPs) have an excellent hypoglycemic effect and can effectively inhibit α-glucosidase, which is the therapeutic target enzyme for type 2 diabetes mellitus. However, its hypoglycemic components and molecular mechanisms remain unclear, and its stability in food pro...

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Autores principales: Li, Zhiming, Zhang, Shu, Meng, Weihong, Zhang, Jiayu, Zhang, Dongjie
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10649794/
https://www.ncbi.nlm.nih.gov/pubmed/37959088
http://dx.doi.org/10.3390/foods12213970
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author Li, Zhiming
Zhang, Shu
Meng, Weihong
Zhang, Jiayu
Zhang, Dongjie
author_facet Li, Zhiming
Zhang, Shu
Meng, Weihong
Zhang, Jiayu
Zhang, Dongjie
author_sort Li, Zhiming
collection PubMed
description Hydrolysates of coix seed prolamins (CHPs) have an excellent hypoglycemic effect and can effectively inhibit α-glucosidase, which is the therapeutic target enzyme for type 2 diabetes mellitus. However, its hypoglycemic components and molecular mechanisms remain unclear, and its stability in food processing needs to be explored. In this study, four potential α-glucosidase inhibitory peptides (LFPSNPLA, FPCNPLV, HLPFNPQ, LLPFYPN) were identified and screened from CHPs using LC-MS/MS and virtual screening techniques. The results of molecular docking showed that the four peptides mainly inhibited α-glucosidase activity through hydrogen bonding and hydrophobic interactions, with Pro and Leu in the peptides playing important roles. In addition, CHPs can maintain good activity under high temperatures (40~100 °C) and weakly acidic or weakly alkaline conditions (pH 6.0~8.0). The addition of glucose (at 100 °C) and NaCl increased the inhibitory activity of α-glucosidase in CHPs. The addition of metal ions significantly decreased the inhibitory activity of α-glucosidase by CHPs, and their effects varied in magnitude with Cu(2+) having the largest effect followed by Zn(2+), Fe(3+), K(+), Mg(2+), and Ca(2+). These results further highlight the potential of CHPs as a foodborne hypoglycemic ingredient, providing a theoretical basis for the application of CHPs in the healthy food industry.
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spelling pubmed-106497942023-10-30 Screening and Activity Analysis of α-Glucosidase Inhibitory Peptides Derived from Coix Seed Prolamins Using Bioinformatics and Molecular Docking Li, Zhiming Zhang, Shu Meng, Weihong Zhang, Jiayu Zhang, Dongjie Foods Article Hydrolysates of coix seed prolamins (CHPs) have an excellent hypoglycemic effect and can effectively inhibit α-glucosidase, which is the therapeutic target enzyme for type 2 diabetes mellitus. However, its hypoglycemic components and molecular mechanisms remain unclear, and its stability in food processing needs to be explored. In this study, four potential α-glucosidase inhibitory peptides (LFPSNPLA, FPCNPLV, HLPFNPQ, LLPFYPN) were identified and screened from CHPs using LC-MS/MS and virtual screening techniques. The results of molecular docking showed that the four peptides mainly inhibited α-glucosidase activity through hydrogen bonding and hydrophobic interactions, with Pro and Leu in the peptides playing important roles. In addition, CHPs can maintain good activity under high temperatures (40~100 °C) and weakly acidic or weakly alkaline conditions (pH 6.0~8.0). The addition of glucose (at 100 °C) and NaCl increased the inhibitory activity of α-glucosidase in CHPs. The addition of metal ions significantly decreased the inhibitory activity of α-glucosidase by CHPs, and their effects varied in magnitude with Cu(2+) having the largest effect followed by Zn(2+), Fe(3+), K(+), Mg(2+), and Ca(2+). These results further highlight the potential of CHPs as a foodborne hypoglycemic ingredient, providing a theoretical basis for the application of CHPs in the healthy food industry. MDPI 2023-10-30 /pmc/articles/PMC10649794/ /pubmed/37959088 http://dx.doi.org/10.3390/foods12213970 Text en © 2023 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Li, Zhiming
Zhang, Shu
Meng, Weihong
Zhang, Jiayu
Zhang, Dongjie
Screening and Activity Analysis of α-Glucosidase Inhibitory Peptides Derived from Coix Seed Prolamins Using Bioinformatics and Molecular Docking
title Screening and Activity Analysis of α-Glucosidase Inhibitory Peptides Derived from Coix Seed Prolamins Using Bioinformatics and Molecular Docking
title_full Screening and Activity Analysis of α-Glucosidase Inhibitory Peptides Derived from Coix Seed Prolamins Using Bioinformatics and Molecular Docking
title_fullStr Screening and Activity Analysis of α-Glucosidase Inhibitory Peptides Derived from Coix Seed Prolamins Using Bioinformatics and Molecular Docking
title_full_unstemmed Screening and Activity Analysis of α-Glucosidase Inhibitory Peptides Derived from Coix Seed Prolamins Using Bioinformatics and Molecular Docking
title_short Screening and Activity Analysis of α-Glucosidase Inhibitory Peptides Derived from Coix Seed Prolamins Using Bioinformatics and Molecular Docking
title_sort screening and activity analysis of α-glucosidase inhibitory peptides derived from coix seed prolamins using bioinformatics and molecular docking
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10649794/
https://www.ncbi.nlm.nih.gov/pubmed/37959088
http://dx.doi.org/10.3390/foods12213970
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