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<p>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.</p><p></p>

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Screening and analysis of malt pentapeptide DPP-IV inhibitory activity

  • 期刊论文

  • 出版模式：

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  • 发表日期：

    2025年11月12日

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  • Yi He,
  • Yan Zhang,
  • Pengying Zhang,
  • Jiaying Li,
  • Wannan Li,
  • Weiwei Han

摘要

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 (IC50: 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.