Stability, Bioavailability, and Structure–Activity Relationship of Casein-Derived Peptide YPVEPF with a Sleep-Enhancing Effect,Journal of Agricultural and Food Chemistry

当前位置： X-MOL 学术 › J. Agric. Food Chem. › 论文详情

Our official English website, www.x-mol.net, welcomes your feedback! (Note: you will need to create a separate account there.)

Stability, Bioavailability, and Structure–Activity Relationship of Casein-Derived Peptide YPVEPF with a Sleep-Enhancing Effect
Journal of Agricultural and Food Chemistry ( IF 5.7 ) Pub Date : 2022-11-16 , DOI: 10.1021/acs.jafc.2c05024
Jingjing Qian ₁ , Lin Zheng ₁ , Yijun Zhao ₂ , Mouming Zhao _{1,

2,

3}

Affiliation

YPVEPF (Tyr-Pro-Val-Glu-Pro-Phe) is an outstanding sleep-enhancing peptide derived from casein. This study aimed to evaluate the bioavailability of YPVEPF in vitro and in vivo and to explore its structure–activity relationship through a sleep test and cheminformatics. Our results showed that YPVEPF was unstable against gastrointestinal enzymes and almost totally degraded to YPVEP in vitro. However, the pharmaco-kinetics results in vivo showed that the C_max of YPVEPF was 10.38 ± 4.01 ng/mL at 5 min, and YPVEPF could be detected in the stomach, intestine, and brain at 12.89 ± 0.55, 10.26 ± 0.23, and 2.47 ± 0.55 ng/g, respectively. The main metabolites including YPVEP, YP, PVEPF, and PVEP were identified. We first explored whether the fragment YPVEP also had a strong sleep-enhancing effect, and the sleep-enhancing effects of PVEPF and PVEP (lacking a Tyr residue) significantly decreased compared with those of YPVEPF and YPVEP. Moreover, molecular docking and quantum calculations revealed that the N-terminus Tyr played a dominant role in YPVEPF and YPVEP. They had distinctive self-folding structures and varying electron-withdrawing properties of the groups at the N terminus, allowing different binding modes and electron/proton transfer.

中文翻译：

具有促睡眠作用的酪蛋白衍生肽 YPVEPF 的稳定性、生物利用度和构效关系

YPVEPF (Tyr-Pro-Val-Glu-Pro-Phe) 是一种源自酪蛋白的出色的睡眠增强肽。本研究旨在评估 YPVEPF 在体外和体内的生物利用度，并通过睡眠测试和化学信息学探索其结构-活性关系。我们的结果表明 YPVEPF 对胃肠道酶不稳定，并且在体外几乎完全降解为 YPVEP。然而，体内药代动力学结果表明，C _max5 分钟时 YPVEPF 的浓度为 10.38 ± 4.01 ng/mL，在胃、肠和脑中的 YPVEPF 浓度分别为 12.89 ± 0.55、10.26 ± 0.23 和 2.47 ± 0.55 ng/g。鉴定了主要代谢物，包括 YPVEP、YP、PVEPF 和 PVEP。我们首先探讨了片段 YPVEP 是否也有很强的睡眠增强作用，与 YPVEPF 和 YPVEP 相比，PVEPF 和 PVEP（缺少 Tyr 残基）的睡眠增强作用显着降低。此外，分子对接和量子计算表明，N 端 Tyr 在 YPVEPF 和 YPVEP 中起主导作用。它们具有独特的自折叠结构和 N 末端基团的不同吸电子特性，允许不同的结合模式和电子/质子转移。

更新日期：2022-11-16

点击分享查看原文

点击收藏

阅读更多本刊最新论文本刊介绍/投稿指南11