ArticleAmino acids2024
A novel ACE inhibitory peptide from Pelodiscus sinensis Wiegmann meat water-soluble protein hydrolysate.
Article in Amino acids, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers, 1 of them a synthesis that pooled it.
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Who cites it
7 citing papers in PubMed, 1 synthesis or guideline pooled it.
- Food-Derived Antihypertensive Peptides: Mechanisms, Multi-Methodological Approaches, Bioavailability, and Functional Food Applications.Molecules (Basel, Switzerland) · 2026Pooled it
- Proteomics-Guided Computational Prioritization of Putative RANKL-Binding Peptides from Proteins Identified in Deer Horn Glue.International journal of molecular sciences · 2026Article
- The Isolation and Characterization of ACE Inhibitory Peptides fromFoods (Basel, Switzerland) · 2026Article
- Bioactive Peptides from Soft-Shelled Turtle: Extraction, Preparation and Biological Activities.Foods (Basel, Switzerland) · 2026Review
- Optimization of the Microbial-Enzymatic Synergistic Treatment of Cottonseed Protein and Evaluation of the Nutritional Value and Antioxidant Activity of Cottonseed Peptides.Foods (Basel, Switzerland) · 2026Article
- ACE-Inhibitory Peptides from Yanbian Cattle Hemoglobin: Screening, Kinetics, and Molecular Dynamics Simulation.Foods (Basel, Switzerland) · 2026Article
- A near-telomere-to-telomere genome assembly of the Chinese soft-shelled turtle (Pelodiscus sinensis).Scientific data · 2026Article
Corrections and comments
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Pelodiscus sinensis meat is a nutritional food and tonic with angiotensin-converting enzyme (ACE) inhibitory activities. To identify the bioactive substances responsible, several bioinformatics methods were integrated to enable a virtual screening for bioactive peptides in proteins identified within a water-soluble protein fraction of Pelodiscus sinensis meat by Shotgun proteomics. The peptides were generated from the identified proteins by in silico proteolysis using six proteases. A comparison of the numbers of proteins suitable for digestion with each enzyme and the iBAQ (intensity-based absolute quantification) values for these proteins revealed that bromelain and papain were the most suitable proteases for this sample. Next, the water solubility, toxicity, and ADMET (absorption/distribution/metabolism/excretion/toxicity) properties of these peptides were evaluated in silico. Finally, a novel ACE inhibitory peptide IEWEF with an IC
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.