Novel ACE Inhibitory Peptides Derived from Yeast Hydrolysates: Screening, Inhibition Mechanisms and Effects on HUVECs

被引：30
作者：
Huang, Yanbo [1 ,2 ]
Jia, Feng [1 ]
Zhao, Jinsong [1 ]
Hou, Yi [2 ]
Hu, Song-Qing [1 ]
机构：
[1] South China Univ Technol, Overseas Expertise Intro Ctr Discipline Innovat F, Sch Food Sci & Engn, Guangzhou 510641, Peoples R China
[2] South China Univ Technol, State Key Lab Pulp & Paper Engn, Guangzhou 510641, Guangdong, Peoples R China
来源：
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY | 2021年 / 69卷 / 08期
关键词：
angiotensin-converting enzyme; yeast hydrolysate; peptide; in silico; human umbilical vein endothelial cells; high-throughput sequencing; I-CONVERTING-ENZYME; SOLUBLE GUANYLATE-CYCLASE; NITRIC-OXIDE PRODUCTION; ANTIHYPERTENSIVE ACTIVITY; ENDOTHELIAL-CELLS; PROTEIN; PURIFICATION; EXPRESSION; IDENTIFICATION; ACTIVATION;
D O I：
10.1021/acs.jafc.0c06053
中图分类号：
S [农业科学];
学科分类号：
09 ;
摘要：
The antihypertensive activity of yeast hydrolysate (YH) was confirmed in our previous study. However, the critical peptides in YH and the underlying mechanisms have not been fully elucidated. This study aimed to explore the angiotensin-converting enzyme (ACE) inhibitory peptides in YH and illustrate their molecular and cellular mechanisms. The potential of YH-derived peptides was evaluated by in silico methods, followed by in vitro verification. A new competitive ACE inhibitory peptide, VIPVPFF (V7), with an IC50 value of 10.27 mu M, was screened. YH and V7 increased the nitric oxide (NO) levels, upregulated GUCY1A1 gene expression (approximately 15-fold), and functioned in several hypertension-related pathways in human umbilical vein endothelial cells (HUVECs). This study revealed the antihypertensive mechanisms of YH and V7, laying down a theoretical basis for their application.
引用
收藏
页码：2412 / 2421
页数：10
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