| DFBP ID - DFBPACEI2027(ACE-inhibitory peptide) |
| DFBP ID |
DFBPACEI2027 |
| Peptide sequence |
YV |
| Type |
Native peptide |
| Peptide/Function name |
ACE-inhibitory peptide |
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| Function-activity relationship |
| Main bioactivity |
ACE-inhibitory activity |
| Otheir bioactivity |
Antihypertensive activity [D1], Multifunctional activity [D2] |
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| Calculated physicochemical properties |
| Three-letter amino acid |
Tyr-Val |
| Single-letter amino acid |
YV |
| Peptide length |
2 |
| Peptide mass |
| Experimental mass |
Theoretical mass |
| 300 Da |
280.32 Da c |
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| Net charge |
0.00 c |
| Isoelectric point (pI) |
5.92 c |
| IC50 |
63.97 μg/mL (= 213.23 μM) |
| pIC50 |
-1.806 |
| GRAVY |
1.4500 c |
| Hydrophilic residue ratio |
50% c |
| Peptide calculator |
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| Biological/Functional activity & target protein |
| ACE-inhibitory activity |
The peptide YV showed moderate Angiotensin-Converting Enzyme (ACE) (EC 3.4.15.1) inhibitory activity with an IC50 value of 63.97 μg/mL (= 213.23 μM).
Using a Lineweaver-Burk plot, YV was determined to be a competitive inhibitor, and the inhibition constant (Ki) was found to be 55.20 μg/mL.
The molecular docking analysis revealed that the binding between YV and the S1 and S2 pocket sites of ACE was mainly stabilized by a hydrogen bond.
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| Specific target protein(s) |
Specific Target Protein(s): Angiotensin-converting enzyme |
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| Taste properties & Structure |
| Bitterness |
| Literature report |
N.D |
| Bitter prediction tools |
Bitter taste prediction |
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| SMILES |
N[C@@]([H])(Cc1ccc(O)cc1)C(=O)N[C@@]([H])(C(C)C)C(=O)O |
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| Preparation method |
| Mode of preparation |
Enzymatic hydrolysis
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| Enzyme(s)/starter culture |
The purified ovalbumin was subjected to alkaline hydrolysis (0.25 M NaOH) at 40 ℃ for 2–10 h. The best ACE-inhibitory activity was observed at 8 h of hydrolysis. |
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| Stability & Cytotoxicity |
| Peptide stability |
| Literature report: |
The peptide YV maintained ACE inhibitory activity after gastrointestinal digestion.
An in vitro test of intestinal absorption showed that YV had a high potential for absorption into the Caco-2 cell monolayer model.
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| EHP-Tool: |
Enzymatic Hydrolysis Prediction Tool (EHP-Tool) |
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| Peptide cytotoxicity |
| Literature report: |
The peptide YV showed no cytotoxic effects on human red blood cells, human keratinocyte cells (HaCaT) and human lung fibroblasts cells (MRC-5).
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| Prediction: |
ToxinPred |
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| Additional information |
| Additional information |
The ACE-inhibitory activity of YV could provide potential candidates for developing supplementary and therapeutic agents against hypertension. |
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| Database cross-references |
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| Reference(s) |
| Primary literature |
Khueychai, S., Jangpromma, N., Choowongkomon, K., Joompang, A., Daduang, S., Vesaratchavest, M., et al. A novel ACE inhibitory peptide derived from alkaline hydrolysis of ostrich (Struthio camelus) egg white ovalbumin. Process Biochemistry. 2018, 73, 235-45.
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| Other literature(s) |
N.D |
| PubDate |
2018 |
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