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Updated: Jun 27, 2026

Peptide-based Identification of Functional Motifs and their Binding Partners
Published on: June 30, 2013
Novel ACE Inhibitory Peptides Derived from Yeast Hydrolysates: Screening, Inhibition Mechanisms and Effects on HUVECs
Yanbo Huang1,2, Feng Jia1, Jinsong Zhao1
1Overseas Expertise Introduction Center for Discipline Innovation of Food Nutrition and Human Health (111 Center), School of Food Sciences and Engineering, South China University of Technology, Guangzhou 510641, Guangdong, China.
Abstract:
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 μM, 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.
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