ArticleScientific reports2026
Bee pollen-derived peptide with dual DPP-IV Inhibition and glucose transport modulation.
Article in Scientific reports, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
1 citing paper in PubMed.
- Ensemble Machine Learning- and Deep Learning-Driven Identification and Validation of Sennidin B as a Novel Dipeptidyl Peptidase-4 Inhibitor.International journal of molecular sciences · 2026Article
Corrections and comments
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Authors and funding
8 authors.
Funding
Abstract
This study investigates the potential of bee pollen protein hydrolysate (BPPH) as a natural source of bioactive peptides capable of inhibiting dipeptidyl peptidase IV (DPP-IV) for the management of type 2 diabetes mellitus (T2DM), a metabolic disorder characterized by insulin resistance and hyperglycemia. BPPH was generated through pepsin–pancreatin digestion, followed by ultrafiltration and RP-HPLC purification. LC-Q-TOF-MS/MS analysis identified Ala-Thr-His-Ala-Leu-Leu-Ala (ATHALLA, AA-7) as a predominant peptide associated with DPP-IV inhibitory activity. AA-7 exhibited strong DPP-IV inhibitory activity (IC50 = 52.63 ± 2.32 µM) relative to the reference inhibitor diprotin A (IC50 = 22.4 ± 1.29 µM). Molecular docking predicted stable binding of AA-7 within the DPP-IV catalytic pocket, mediated by hydrogen bonding and hydrophobic interactions with key residues. AA-7 also modulated glucose uptake in Caco-2 cells, influencing SGLT1 and GLUT2 gene expression in a dose-dependent manner. Docking analysis suggested potential interactions with selected SGLT1 and GLUT2 residues, providing structural support for the observed cellular responses rather than definitive mechanistic evidence. In silico ADMET analysis indicated poor passive membrane permeability and limited predicted intestinal absorption, along with minimal CYP450 interactions and low predicted toxicity, highlighting potential pharmacokinetic limitations while supporting a favorable safety profile. These findings highlight AA-7 as a dual-action peptide with demonstrated DPP-IV inhibitory activity and the ability to modulate glucose transport in vitro, supporting the potential of bee-pollen-derived peptides for glycemic regulation and functional food or nutraceutical applications.
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What Socratic holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the Socratic graph.