Department of Plant, Food and Environmental Sciences, Faculty of Agriculture, Dalhousie University, Truro, Nova Scotia B2N 5E3, Canada.
Department of Chemistry and Biomolecular Sciences, University of Ottawa, Ottawa, Ontario K1N 6N5, Canada.
J Agric Food Chem. 2024 Sep 18;72(37):20527-20536. doi: 10.1021/acs.jafc.4c06539. Epub 2024 Sep 4.
This study aimed to test the hypothesis that bioactive peptides can exert multiple bioactivities at different sites in the gastrointestinal tract. Our previous research identified 33 gastric-resistant peptides derived from wheat germ with potential antiadhesive activity against in the stomach. In this work, in silico digestion of these peptides with trypsin, thermolysin, and chymotrypsin produced 67 peptide fragments. Molecular docking was conducted to predict their ACE and DPP-IV inhibitory activities in the small intestine. Three peptides (VPIPNPSGDR, VPY, and AR) were selected and synthesized for in vitro validation. Their generation in the gastrointestinal tract was verified via in vitro digestion, followed by mass spectrometry analysis. The IC values for ACE inhibition were 199.5 μM (VPIPNPSGDR), 316.3 μM (VPY), and 446.7 μM (AR). For DPP-IV inhibition, their IC values were 0.5, 1.6, and 4.0 mM, respectively. This research pioneers new directions in the emerging field of multifunctional peptides, providing scientific evidence to support the utilization of wheat germ as value-added food ingredients.
本研究旨在验证生物活性肽可在胃肠道的不同部位发挥多种生物活性的假设。我们之前的研究从麦芽中鉴定出 33 种具有胃内抗粘附活性的胃抵抗肽。在这项工作中，用胰蛋白酶、嗜热菌蛋白酶和糜蛋白酶对这些肽进行计算机模拟消化，产生了 67 个肽片段。通过分子对接预测它们在小肠中的 ACE 和 DPP-IV 抑制活性。选择并合成了三个肽（VPIPNPSGDR、VPY 和 AR）进行体外验证。通过体外消化和质谱分析验证了它们在胃肠道中的生成。ACE 抑制的 IC 值分别为 199.5 μM（VPIPNPSGDR）、316.3 μM（VPY）和 446.7 μM（AR）。对于 DPP-IV 抑制，其 IC 值分别为 0.5、1.6 和 4.0 mM。这项研究为多功能肽这一新兴领域开辟了新的方向，为利用麦芽作为有价值的食品成分提供了科学依据。
