Dipeptidyl peptidase IV (DPP-IV) is involved in incretin hormone processing and therefore plays a key role in glycemic regulation. This review summarizes the latest developments in food protein-derived DPP-IV inhibitory peptides. The in silico approaches currently used to develop targeted strategies for the enzymatic release of DPP-IV inhibitory peptides from food proteins are outlined. The features within the primary sequences of potent DPP-IV inhibitory di-, tri-, and larger peptides, having half maximal inhibitory activity (IC50) < 100 µM, were evaluated and the outcomes are presented herein. It is proposed that detailed analysis of those food derived peptides identified in humans following ingestion may constitute a practical strategy for the targeted identification of novel bioavailable DPP-IV inhibitory peptides. Human intervention studies are required as the specific role of food protein-derived DPP-IV inhibitory peptides in the regulation of glycaemia in humans remains to be fully elucidated.

Practical applications
This review provides recent information on dipeptidyl peptidase IV (DPP-IV) inhibitory peptides arising from food protein hydrolysates. Small animal studies have demonstrated that food protein hydrolysates with in vitro DPP-IV inhibitory properties also display antidiabetic activity. DPP-IV inhibitory peptides may be used as food ingredients to improve glycemic regulation in Type 2 diabetics. Therefore, the development of potent DPP-IV inhibitory hydrolysates containing bioavailable peptides in humans is of significant interest. This may help in the formulation of foods containing physiologically relevant doses of bioactive hydrolysates/peptides. Acquisition of detailed knowledge of DPP-IV inhibitory peptide features via the utilization of in silico tools may help to optimize the release of potent DPP-IV inhibitory peptides during enzymatic hydrolysis of food proteins. This review provides information on features within the primary sequences of potent DPP-IV inhibitory peptides and current in silico strategies which may be used to inform on the targeted enzymatic hydrolysis of food proteins.

Features of dipeptidyl peptidase IV (DPP-IV) inhibitory peptides from dietary proteins.

Identification of novel dipeptidyl peptidase IV (DPP-IV) inhibitory peptides in camel milk protein hydrolysates.

Background Diabetes, which currently affects 1 in 11 adults, is considered one of the biggest worldwide health crises of the 21st century. Over the last decade, synthetic inhibitors of the enzyme dipeptidyl-peptidase IV (DPP-IV) have emerged as an effective pharmaceutical approach for the management of type 2 diabetes. These molecules exert their beneficial effect by preventing the inactivation of gut-derived hormones that play a pivotal role in glycemic regulation. More recently, food components have been suggested as sources of DPP-IV inhibitors with the potential to help manage blood glucose levels. Scope and approach This review examines the sources, production, molecular characteristics and modes of action of food-derived DPP-IV inhibitors. Insights into the needs for future research to validate their efficacy and to establish their application in the management of type 2 diabetes are also discussed. Key findings and conclusions To date, hydrolysates of protein from a variety of food commodities, including both plant and animal sources, have been shown to be able to inhibit the activity of the DPP-IV enzyme. Moreover, a number of peptides, either isolated from these hydrolysates or synthetically produced, as well as non-protein-derived compounds such as polyphenols, have also been identified as DPP-IV inhibitors. These food-derived constituents present different degrees of potency and modes of action on the DPP-IV enzyme. While their effectiveness in humans is currently unknown, findings from in vitro and animal studies conducted to date warrant further research to evaluate their potential as functional food ingredients for glycemic regulation.

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Food-derived dipeptidyl-peptidase IV inhibitors as a potential approach for glycemic regulation : current knowledge and future research considerations

Diabetes is a chronic metabolic disorder which leads to high blood sugar levels over a prolonged period. Type 2 diabetes mellitus (T2DM) is the most common form of diabetes and results from the body’s ineffective use of insulin. Over ten dipeptidyl peptidase IV (DPP-IV) inhibitory drugs have been developed and marketed around the world in the past decade. However, owing to the reported adverse effects of the synthetic DPP-IV inhibitors, attempts have been made to find DPP-IV inhibitors from natural sources. Food-derived components, such as protein hydrolysates (peptides), have been suggested as potential DPP-IV inhibitors which can help manage blood glucose levels. This review focuses on the methods of discovery of food-derived DPP-IV inhibitory peptides, including fractionation and purification approaches, in silico analysis methods, in vivo studies, and the bioavailability of these food-derived peptides. Moreover, food-derived DPP-IV inhibitory peptides discovered during this decade are listed and distributed in a 3D scatter plot graph based on their IC50, molecular weight, and grand average of hydropathicity values, which can help us to understand the relationship between the features of the peptides and their activities.

Discovery of Food-Derived Dipeptidyl Peptidase IV Inhibitory Peptides: A Review

New dipeptidyl peptidase IV (DPP-IV)-inhibitory peptides from trypsin/chymotrypsin-treated goat milk casein hydrolysates were isolated and identified by two-dimensional silica thin-layer chromatography (2D-TLC) combined to nano LC-MS/MS 2D-TLC with chloroform/methanol/25% ammonia (2:2:1) and n-butanol/acetic acid/water (4:1:1) as the first- and second-dimension eluents, respectively, in analytical and semipreparative scales, was set up and verified by reversed-phase high-performance liquid chromatography (RP-HPLC) to be feasible and efficient to separate the hydrolysates Five new DPP-IV-inhibitory peptides, four relatively large oligopeptides (MHQPPQPL, SPTVMFPPQSVL, VMFPPQSVL, and INNQFLPYPY), and AWPQYL were identified, and INNQFLPYPY showed a notable IC50 value of 4008 μM as an uncompetitive inhibitor Interactive effects on DPP-IV inhibition were also observed among separated fractions and pure synthetic peptide mixtures with concentration-dependent activity The study gives new insights into goat casein hydrolysates with identified DPP-IV-inhibitory peptides efficiently isolated by 2D-TLC, which provides a simple and cost-efficient separation process and is compatible with liquid chromatography-tandem mass spectrometry (LC-MS/MS) identification

Isolation and Identification of Dipeptidyl Peptidase IV-Inhibitory Peptides from Trypsin/Chymotrypsin-Treated Goat Milk Casein Hydrolysates by 2D-TLC and LC-MS/MS.

Synergistic inhibition of human dipeptidyl peptidase IV by combinations of peptides

Analyzing a dipeptide library to identify human dipeptidyl peptidase IV inhibitor

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Synergistic inhibition of human dipeptidyl peptidase IV by combinations of peptides

Analyzing a dipeptide library to identify human dipeptidyl peptidase IV inhibitor