In vitro inhibition of platelet aggregation by peptides derived from oat (Avena sativa L.), highland barley (Hordeum vulgare Linn. var. nudum Hook. f.), and buckwheat (Fagopyrum esculentum Moench) proteins

Abstract

Bioactive compounds present in foods could have beneficial effects on human health. In this study, we report the capacity of peptides released from oat, highland barley, and buckwheat proteins after enzymatic digestion to inhibit platelet aggregation in vitro. All hydrolysates showed high antiplatelet activity, with IC50 values of 0.282mg/ml (oat flour gastrointestinal hydrolysate, 6h) to 2.496mg/ml (highland barley glutelin tryptic hydrolysate, 14h) in a dose-dependent manner. Thirty-eight peptides with more than seven residues were identified in the tryptic hydrolysates of oat globulin. Results of computational modeling revealed that nine peptides, including ALPIDVLANAYR, EFLLAGNNKR, GEEFGAFTPK, QLAQIPR, LQAFEPLR, ALPVDVLANAYR, GEEFDAFTPK, QKEFLLAGNNK, and TNPNSMVSHIAGK bound the cyclooxygenase-1 active centers with low binding energy (-6.5 to -7.5kcal/mol). This is the first report to identify antiplatelet peptides from grain hydrolysates and the binding modes at the molecular level, leading to their possible use as functional food ingredients to prevent thrombosis.

Keywords: Acetylsalicylic acid (PubChem CID: 2244); Arachidonic acid (PubChem CID: 444899); Arginine (PubChem CID: 6322); COX1; Computational modeling; Glutamic acid (PubChem CID: 33032); Grain; LC–MS; Leucine (PubChem CID: 6061); Serine (PubChem CID: 5951); Sodium citrate (PubChem CID: 6224); Thrombosis; Thromboxane A(2) (PubChem CID: 5280497); Thromboxane B(2) (PubChem CID: 5283137); Trypsin; Tyrosine (PubChem CID: 6057).