In silico investigation of molecular targets, pharmacokinetics, and biological activities of chicken egg ovalbumin protein hydrolysates
Food-derived bioactive peptides are promising ingredients for developing functional foods and nutraceuticals due to their putative safety, low cost, and multiple health benefits. Chicken egg is considered a major source of dietary protein, lipids, vitamins, and minerals but is also highly allergenic. The aim of this work was to investigate the inherent bioactive properties of chicken ovalbumin peptides using in silico approaches. Ovalbumin was in silico hydrolyzed with gastrointestinal proteases (chymotrypsin, trypsin, and pepsin) and results indicated cleavage of the most allergenic protein with an overall 36.62% theoretical degree of hydrolysis, consisting of 132 fragments of which 65 were di-, tri-, tetra- or oligopeptides. The most represented biological targets obtained for these peptides include HLA class I histocompatibility antigen A-3, E3 ubiquitin-protein ligase XIAP, and angiotensin-converting enzyme. Notably, peptides AIVF and AVL were found to have multi-target potentials. Gene enrichment analysis showed interaction of these peptides with some kinases and transcription factors. Overall, results from binding affinity, pharmacokinetics and physicochemical properties, and therapeutic activity showed that PGF, SSL, GGL, AVL, VY, and IL are promising peptide candidates for further studies. These results are important in the design of peptide-based functional foods and therapeutic products devoid of allergenic property of ovalbumin.