Screening and analysis of malt pentapeptide DPP-IV inhibitory activity

Type 2 diabetes mellitus (T2DM) poses a significant global health burden, with dipeptidyl peptidase-IV (DPP-IV) inhibitors being critical therapeutic targets for its management. Malt, a natural medicinal food, shows promise for T2DM treatment, yet its active compounds need further exploration. This study integrates molecular docking (Libdock, Autodock Vina), deep learning models (ConPlex, KPGT), molecular dynamics (MD) simulations, and network pharmacology to identify and validate DPP-IV inhibitors from malt. The pentapeptide YPQPQ, derived from malt hordein, exhibited potent DPP-IV inhibition (IC<sub>50</sub>: 23.87 μM) in vitro. Network pharmacology identified MAPK1 and MAPK3 (ERK1 and ERK2) as key targets, with YPQPQ significantly reducing ERK phosphorylation. Molecular dynamics (MD) simulations revealed YPQPQ's binding similarity to Diprotin A. These findings establish YPQPQ as a novel natural DPP-IV inhibitor, modulating the ERK signaling pathway, offering potential for T2DM therapy.

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Publication Details

Journal
npj Science of Food
Published
2025-11-12
DOI
https://doi.org/10.1038/s41538-025-00584-8
Primary Topic
Peptidase Inhibition and Analysis
Type
article
Field-Weighted Citation Impact
0.00

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article

Screening and analysis of malt pentapeptide DPP-IV inhibitory activity

Weiwei Han, Pengying Zhang, Jiaying Li, Yan Zhang et al.
npj Science of Food
Peptidase Inhibition and Analysis
article

Screening and analysis of malt pentapeptide DPP-IV inhibitory activity

Weiwei Han, Pengying Zhang, Jiaying Li, Yan Zhang, Yi He, Wannan Li
article en

Abstract

Type 2 diabetes mellitus (T2DM) poses a significant global health burden, with dipeptidyl peptidase-IV (DPP-IV) inhibitors being critical therapeutic targets for its management. Malt, a natural medicinal food, shows promise for T2DM treatment, yet its active compounds need further exploration. This study integrates molecular docking (Libdock, Autodock Vina), deep learning models (ConPlex, KPGT), molecular dynamics (MD) simulations, and network pharmacology to identify and validate DPP-IV inhibitors from malt. The pentapeptide YPQPQ, derived from malt hordein, exhibited potent DPP-IV inhibition (IC<sub>50</sub>: 23.87 μM) in vitro. Network pharmacology identified MAPK1 and MAPK3 (ERK1 and ERK2) as key targets, with YPQPQ significantly reducing ERK phosphorylation. Molecular dynamics (MD) simulations revealed YPQPQ's binding similarity to Diprotin A. These findings establish YPQPQ as a novel natural DPP-IV inhibitor, modulating the ERK signaling pathway, offering potential for T2DM therapy.

npj Science of FoodVol. 9(1)
Ministry of Education (KN)
People's Government of Jilin Province
Openalex Percentile: Top 53%
Peptidase Inhibition and Analysis
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Screening and analysis of malt pentapeptide DPP-IV inhibitory activity — Weiwei Han, Pengying Zhang, et al. · npj Science of Food (2025) | TGRS Research Map | TGRS