Peptidomic analysis of anionic oat intestinal peptides

Abstract

Many studies have focused in recent years on the functional and nutritional properties of proteins in cereal and the bran and the bioactive attributes of peptides derived from these proteins. In vitro digestion model in combination with anion exchange chromatography isolates the cereal anionic intestinal peptides which, unlike cereal hydrophobic peptides, has not been proven to strongly relate to the bioactivity of peptides. The aim of my PhD project is to identify the bioactive anionic peptides derived from the storage protein of cereal bran and to assess their bioactivity. The protein was extracted from oat bran, wheat bran and barley and was then subjected to in vitro digestion model. The intestinal digesta of oat bran protein showed highest overall antioxidant and ACE inhibitory activity and was fractionated by anion exchange chromatography, and the fractions of which with highest antioxidant and ACE inhibitory activity were selected for sequencing by R-HPLC-MS/MS. The peptides in the fraction candidates were identified. In addition, the most abundant peptides in the fraction candidates were identified and the relation of those abundant peptides to bioactivity was evaluated. For future perspective, the ACE inhibitory peptide candidates will be analysed by molecular docking. The peptide will be selected for synthesis and assayed to confirm the discovery of the novel peptides. Meanwhile, it is interesting to bring the novel peptides to cell-line works and in vivo.