Discovery of Bifunctional Anti-DPP-IV and Anti-ACE Peptides from Housefly Larval Proteins After In silico Gastrointestinal Digestion

Proteins and peptides of housefly larvae (HFL) have potential applications in food therapy. The fate HFL proteins following human gastrointestinal (GI) digestion is unknown. This study adopted a computational approach to discover released from upon GI digestion. In silico eight major 783 peptides. comprised 243 exhibiting 13 types bioactivities. Ninety-two single-function anti-dipeptidyl peptidase IV (anti-DPP-IV), III, anti-angiotensin converting enzyme (anti-ACE), or antioxidant activity were found. Sixty-three multi-function peptides, encompassing 32 bifunctional anti-DPP-IV anti-ACE Further screening led five non-toxic, non-allergenic, high-GI-absorption dipeptides: AF, GW, GY, PH, VF. Molecular docking found the dipeptides interact with active site DPP-IV through hydrophobic interactions. Only GW VF could bind ACE. Thus, are competitive inhibitors DPP-IV. ACE, whereas PH non-competitive inhibitors. Overall, liberate numerous single- proteins. Hence, can be tapped for antidiabetic antihypertension functional