No abstract

Selected synthetic dipeptides and milk protein hydrolysates were evaluated for their dipeptidyl peptidase IV (DPP-IV) inhibitory properties, and their superoxide (SO) and 2,2-diphenyl-1-picrylhydrazyl (DPPH) radical scavenging activities. DPP-IV inhibition was seen with eight out of the twelve dipeptides and 5 of the twelve hydrolysates studied. Trp-Val inhibited DPP-IV, however, inhibition was not observed with the reverse peptide Val-Trp. The most potent hydrolysate inhibitors were generated from casein (CasH2) and lactoferrin (LFH1). Two Trp containing dipeptides, Trp-Val and Val-Trp, and three lactoferrin hydrolysates scavenged DPPH. The dipeptides had higher SO EC 50 values compared to the milk protein hydrolysates (arising from three lactoferrin and one whey protein hydrolysates). Higher molecular mass fractions of the milk protein hydrolysates were associated with the SO scavenging activity. Trp-Val and one lactoferrin hydrolysate (LFH1) were multifunctional displaying both DPP-IV inhibitory and antioxidant (SO and DPPH scavenging) activities. These compounds may have potential as dietary ingredients in the management of type 2 diabetes by virtue of their ability to scavenge reactive oxygen species and to extend the half-life of incretin molecules.

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 proteinderived 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 (IC 50 ) < 100 mM, 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.