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Abstract <p>A comprehensive phytochemical investigation of the methanol extract from the aerial parts of <i>Lespedeza cuneata</i> resulted in the isolation of 36 compounds, including three new <i>C</i>-glycosyl flavonoids (<b>8</b>, <b>9</b>, and <b>11</b>). Their structures were elucidated using HRFAB-MS, as well as 1D and 2D nuclear magnetic resonance spectroscopy, and the isolated compounds were evaluated for inhibitory activity against protein tyrosine phosphatase 1B (PTP1B) and <i>α</i>-glucosidase. Flavonoids <b>1</b>, <b>17</b>, and <b>21</b> exhibited potent PTP1B inhibition (IC<sub>50</sub> 4.9–9.6 µM). Notably, compounds <b>17</b> and <b>25</b> showed strong <i>α</i>-glucosidase inhibition (IC<sub>50</sub> 6.0 and 5.7 µM, respectively), outperforming the reference drug acarbose. Additionally, benzofuran derivative <b>34</b> (IC<sub>50</sub> 29.2 µM) exhibited uncompetitive <i>α</i>-glucosidase inhibition with a <i>K</i><sub>i</sub> of 2.4 µM. Molecular docking and molecular dynamics studies indicated that compound <b>34</b> binds to an allosteric site of <i>α</i>-glucosidase, supporting its uncompetitive inhibition mechanism. These findings suggest that multiple constituents of <i>L. cuneata</i> contribute to its enzyme inhibitory activities and highlight the plant as a promising natural source of multifunctional enzyme inhibitors with potential applications in diabetes management.</p> Graphical Abstract <p></p>

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Polyphenols from the aerial parts of Lespedeza cuneata and their inhibitory effects on PTP1B and α-glucosidase: insights from in vitro and in Silico analyses

  • 期刊论文

  • 发表日期：

    2026年1月28日

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  • Thi Nguyet Anh Dinh,
  • Thi Ly Pham,
  • Viet Phong Nguyen,
  • Taeho Lee,
  • Byung Sun Min,
  • Jeong Ah Kim

摘要

Abstract

A comprehensive phytochemical investigation of the methanol extract from the aerial parts of Lespedeza cuneata resulted in the isolation of 36 compounds, including three new C-glycosyl flavonoids (8, 9, and 11). Their structures were elucidated using HRFAB-MS, as well as 1D and 2D nuclear magnetic resonance spectroscopy, and the isolated compounds were evaluated for inhibitory activity against protein tyrosine phosphatase 1B (PTP1B) and α-glucosidase. Flavonoids 1, 17, and 21 exhibited potent PTP1B inhibition (IC50 4.9–9.6 µM). Notably, compounds 17 and 25 showed strong α-glucosidase inhibition (IC50 6.0 and 5.7 µM, respectively), outperforming the reference drug acarbose. Additionally, benzofuran derivative 34 (IC50 29.2 µM) exhibited uncompetitive α-glucosidase inhibition with a Ki of 2.4 µM. Molecular docking and molecular dynamics studies indicated that compound 34 binds to an allosteric site of α-glucosidase, supporting its uncompetitive inhibition mechanism. These findings suggest that multiple constituents of L. cuneata contribute to its enzyme inhibitory activities and highlight the plant as a promising natural source of multifunctional enzyme inhibitors with potential applications in diabetes management.

Graphical Abstract