ArticleFood chemistry: X2022
Interaction mechanism of three egg protein derived ACE inhibitory tri-peptides and DPPC membrane using FS, FTIR, and DSC studies.
Article in Food chemistry: X, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
3 citing papers in PubMed, 23 citations in OpenAlex.
- Liposome encapsulation for casein-derived peptides: Release behavior,Food chemistry: X · 2025Article
- Identification of a Novel ACE Inhibitory Hexapeptide from Camellia Seed Cake and Evaluation of Its Stability.Foods (Basel, Switzerland) · 2023Article
- Calcium-binding properties, stability, and osteogenic ability of phosphorylated soy peptide-calcium chelate.Frontiers in nutrition · 2023Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Understanding the interaction of food derived angiotensin converting enzyme (ACE) inhibitory peptides and intestinal epithelial cell membrane may help to improve their absorption. This research aimed to study the molecular interaction of ACE inhibitory tri-peptides ADF, FGR, and MIR with DPPC membrane during absorption process. The DPPC liposome was prepared and characterized, then used as a model membrane. The permeability of tri-peptides across the membrane was investigated using Fluorescence spectroscopy. The effect of tri-peptides on the structure and dynamics of DPPC bilayers was determined using Fourier transform infrared spectroscopy. The effect of tri-peptides on the phase transition temperature in the DPPC membrane was also analyzed using Differential scanning calorimetry. The results showed that ACE inhibitory tri-peptides ADF, FGR, and MIR can penetrate into both the membrane-water interface and hydrophobic region of DPPC bilayer, and the tri-peptide FGR have higher permeability across the membrane.
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Registered trials
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