水解物
血管紧张素II
肽
血管平滑肌
蛋白酵素
肾素-血管紧张素系统
血管紧张素转换酶
酪蛋白
化学
生物化学
内科学
酶
内分泌学
生物
药理学
医学
受体
血压
平滑肌
水解
作者
Zijiao Qiao,Jiaqi Wang,Zeqi He,Lina Pan,Konglong Feng,Xiaoyu Peng,Qianru Lin,Yu Gao,Mingyue Song,Sufang Cao,Yunjiao Chen,Yong Cao,Lei Guo
标识
DOI:10.3389/fnut.2022.878768
摘要
Hypertension is a major risk factor leading to cardiovascular disease, and is frequently treated with angiotensin I-converting enzyme (ACE) inhibitory peptides. The objective of this study was to separate and identify an ACE-inhibitory peptide from goat milk casein hydrolysates, and to evaluate its potential for improving angiotensin II (Ang II)-mediated adverse effects on vascular smooth muscle cells (VSMCs). A novel ACE-inhibitory peptide with the highest activity from the goat milk casein hydrolysates as determined by four steps of RP-HPLC was purified and identified as Phe-Pro-Gln-Tyr-Leu-Gln-Tyr-Pro-Tyr (FPQYLQYPY). The results of inhibitory kinetics studies indicated that the peptide was a non-competitive inhibitor against ACE. Gastrointestinal digest in vitro analysis showed that the hydrolysate of FPQYLQYPY was still active after digestion with gastrointestinal proteases. Moreover, we found that the peptide could significantly inhibit the proliferation and migration of Ang II-stimulated VSMCs. Further transcriptomic analysis revealed that differentially expressed genes (DEGs) were enriched in the cardiovascular disease-related pathways, and that the peptide may have the ability to regulate vascular remodeling. Our findings indicate the potential anti-hypertensive effects of FPQYLQYPY, as well-implicate its role in regulating vascular dysfunction.
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