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Journal of the Science of Food and Agriculture· 2026Q1

Apiin from sugarcane leaves modulates postprandial hyperglycemia by targeting dipeptidyl peptidase IV, α ‐amylase, and α ‐glucosidase

Ruotong Kan, Yingcai Zhao, Biqian Wei, Li Zhan et al.

Short summary

Apiin, a compound from sugarcane leaves, significantly reduces postprandial hyperglycemia by inhibiting DPP-IV, α-amylase, and α-glucosidase, as shown in enzyme assays and insulin-resistant mice.

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Key points

  • Apiin from sugarcane leaves shows significant inhibitory activity against DPP-IV, α-amylase, and α-glucosidase.
  • In vitro IC50 values for apiin were 0.21 ± 0.02 mg/mL (DPP-IV), 0.10 ± 0.01 mg/mL (α-amylase), and 0.14 ± 0.02 mg/mL (α-glucosidase).
  • Molecular docking suggests hydrogen bonding is key for apiin's interaction with DPP-IV and α-amylase, while hydrophobic interactions are important for α-glucosidase.
  • Oral apiin administration reduced postprandial blood glucose excursion and the area under the glucose curve in insulin-resistant mice.

AI-generated from the title and abstract; the full text is not read.

Abstract

Abstract BACKGROUND Postprandial hyperglycemia is a metabolic abnormality that can emerge early in the progression toward type 2 diabetes and is closely associated with insulin resistance. Sugarcane leaves, an underutilized by‐product of sugar production, are rich in flavonoids and therefore represent a promising source of bioactive compounds for glycemic control. RESULTS In the present study, 37 phytochemicals previously identified from sugarcane leaves were screened by toxicity prediction and molecular docking against three key targets involved in postprandial glucose regulation, namely dipeptidyl peptidase IV (DPP‐IV), α ‐amylase, and α ‐glucosidase. Apiin was identified as the most promising candidate and was further evaluated by in vitro enzyme inhibition assays and in vivo validation in high‐fat‐diet‐induced insulin‐resistant (IR) mice. Apiin exhibited encouraging inhibitory activity against DPP‐IV, α ‐amylase, and α ‐glucosidase, with IC 50 values of 0.21 ± 0.02, 0.10 ± 0.01 and 0.14 ± 0.02 mg mL −1 , respectively. Molecular docking further indicated that hydrogen bonding played a major role in apiin binding to DPP‐IV and α ‐amylase, whereas hydrophobic and sulfur–X interactions contributed to its recognition by α ‐glucosidase. Oral administration of apiin significantly reduced postprandial blood glucose excursion and decreased the area under the glucose curve in IR mice. CONCLUSION These findings demonstrate that apiin is a major bioactive constituent of sugarcane leaves with the potential to modulate postprandial glucose homeostasis and support the valorization of sugarcane leaves as a functional food resource. © 2026 Society of Chemical Industry.

The authors' abstract, as published at the source. Journal of the Science of Food and Agriculture, 2026 · DOI ↗

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Field: Endocrinology, Diabetes and Metabolism

Endocrinology, Diabetes and MetabolismMedicine