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

Abstract

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.