ArticleFrontiers in nutrition2022
A Novel Angiotensin I-Converting Enzyme Inhibitory Peptide Derived From Goat Milk Casein Hydrolysate Modulates Angiotensin II-Stimulated Effects on Vascular Smooth Muscle Cells.
Article in Frontiers in nutrition, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers, 1 of them a synthesis that pooled it.
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Who cites it
6 citing papers in PubMed, 1 synthesis or guideline pooled it, 19 citations in OpenAlex.
- Bioactive compounds in fermented foods: a systematic narrative review.Frontiers in nutrition · 2025Pooled it
- γ-Glutamylcysteine alleviates hypertension and vascular remodeling in SHR by suppressing oxidative stress through Keap1 S-glutathionylation.Redox report : communications in free radical research · 2026Article
- Isolation, Purification, Identification, and In Vitro ACE Inhibitory Activity of Tyrosine-Arginine Dipeptide From Red Millet Huangjiu.Food science & nutrition · 2026Article
- Goat milk-derived bioactive peptides as a health promoter: an insight based on recent in silico studies.Food science of animal resources · 2026Review
- Therapeutic effect of goat milk and its value-addition: current status and way forward.Journal of food science and technology · 2024Review
- Novel Angiotensin-Converting Enzyme-Inhibitory Peptides Obtained fromBiomolecules · 2024Article
Corrections and comments
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Authors and funding
13 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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
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Registered trials
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