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

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• 作者：Guoyong Yu ; Feng Wang ; Bolin Zhang ; Junfeng Fan ; ^{fanjunfeng@bjfu.edu.cn" class="auth_mail" title="E-mail the corresponding author}
• 关键词：AA ; arachidonic acid ; ASA ; acetylsalicylic acid ; COX1 ; cyclooxygenase-1 ; NS ; normal saline ; PPP ; platelet-poor plasma ; PRP ; platelet-rich plasma ; TXA2 ; thromboxane-A2 ; TXB2 ; thromboxane-B2 ; WP ; washed platelet ; GO ; gastrointestinal hydrolysate of oat flour ; GH ; gastrointestinal hydrolysate of highland barley flour ; GB ; gastrointestinal hydrolysate of buckwheat flour ; TOGB ; tryptic hydrolysate of oat globulin
• 刊名：Food Chemistry
• 出版年：2016
• 出版时间：1 March 2016
• 年：2016
• 卷：194
• 期：Complete
• 页码：577-586
• 全文大小：1494 K

文摘

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 0.282 mg/ml (oat flour gastrointestinal hydrolysate, 6 h) to 2.496 mg/ml (highland barley glutelin tryptic hydrolysate, 14 h) 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 −7.5 kcal/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.