ArticleBiomolecules2022
Identification, Screening, and Comprehensive Evaluation of Novel DPP-IV Inhibitory Peptides from the Tilapia Skin Gelatin Hydrolysate Produced Using Ginger Protease.
Article in Biomolecules, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 15 citations in OpenAlex.
- Circular Valorization of Yellowfin Tuna (Molecules (Basel, Switzerland) · 2026Article
- Food-Derived Antidiabetic Peptides as Multi-Target Systemic Regulators: A Comprehensive Review of Sources, Preparation, Mechanisms and Future Perspectives.Foods (Basel, Switzerland) · 2026Review
- Valorisation of fish scales and bones: a sustainable source of bioactive proteins and collagen for nutraceuticals.Bioresources and bioprocessing · 2025Review
- Identification and In Vitro Evaluation of Milkfish (Foods (Basel, Switzerland) · 2025Article
- Uncovering Novel DPP-IV Inhibitory Peptides from Amphibian (Foods (Basel, Switzerland) · 2025Article
- Preparation and Encapsulation of DPP-IV Inhibitory Peptides: Challenges and Strategies for Functional Food Development.Foods (Basel, Switzerland) · 2025Review
- Article
- Chlorogenic acid: a review on its mechanisms of anti-inflammation, disease treatment, and related delivery systems.Frontiers in pharmacology · 2023Review
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Authors and funding
11 authors at 2 institutions in 1 country.
Funding
Abstract
purposeInhibition of dipeptidyl peptidase-IV (DPP-IV) is an effective therapy for treating type II diabetes (T2D) that has been widely applied in clinical practice. We aimed to evaluate the DPP-IV inhibitory properties of ginger protease hydrolysate (GPH) and propose a comprehensive approach to screen and evaluate DPP-IV inhibitors.
methodsWe evaluated the in vitro inhibitory properties of fish skin gelatin hydrolysates produced by five proteases, namely, neutral protease, alkaline protease, bromelain, papain, and ginger protease, toward DPP-IV. We screened the most potent DPP-IV inhibitory peptide (DIP) using liquid chromatography-tandem mass spectrometry (LC-MS/MS) coupled with in silico analysis. Next, surface plasmon resonance (SPR) technology was innovatively introduced to explore the interactions between DPP-IV and DIP, as well as the IC
resultsGPH displayed the highest degree of hydrolysis (20.37%) and DPP-IV inhibitory activity (65.18%). A total of 292 peptides from the GPH were identified using LC-MS/MS combined with de novo sequencing. Gly-Pro-Hyp-Gly-Pro-Pro-Gly-Pro-Gly-Pro (GPXGPPGPGP) was identified as the most potent DPP-IV inhibitory peptide after in silico screening (Peptide Ranker and molecular docking). Then, the in vitro study revealed that GPXGPPGPGP had a high inhibitory effect on DPP-IV (IC
conclusionOverall, the results suggested that GPH would be a natural functional food for treating T2D and provided new ideas for searching and evaluating potential antidiabetic compounds. The obtained GPXGPPGPGP can be structurally optimized for in-depth evaluation in animal and cellular experiments.
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