DFBP ID - DFBPACEI0131(ACE-inhibitory peptide) |
DFBP ID |
DFBPACEI0131 |
Peptide sequence |
AGS |
Type |
Native peptide |
Peptide/Function name |
ACE-inhibitory peptide |
|
Function-activity relationship |
Main bioactivity |
ACE-inhibitory activity |
Otheir bioactivity |
N.D |
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Calculated physicochemical properties |
Three-letter amino acid |
Ala-Gly-Ser |
Single-letter amino acid |
AGS |
Peptide length |
3 |
Peptide mass |
Experimental mass |
Theoretical mass |
234 Da |
233.22 Da c |
|
Net charge |
0.00 c |
Isoelectric point (pI) |
5.97 c |
IC50 |
0.13 ± 0.03 mg/mL |
pIC50 |
0.886 |
GRAVY |
0.2000 c |
Hydrophilic residue ratio |
66.67% c |
Peptide calculator |
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Biological/Functional activity & target protein |
ACE-inhibitory activity |
The peptide exhibited potent Angiotensin-Converting Enzyme (ACE) (EC 3.4.15.1) inhibitory activity with an IC50
value of 0.13 ± 0.03 mg/mL, and its ACE inhibitory pattern was shown by
Lineweaver–Burk plots to be a non-competitive inhibition pattern.
|
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 |
Non-bitter taste prediction |
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SMILES |
N[C@@]([H])(C)C(=O)NCC(=O)N[C@@]([H])(CO)C(=O)O |
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Preparation method |
Mode of preparation |
Enzymatic hydrolysis |
Enzyme(s)/starter culture |
Hydrolysis with low mocecular weight alkaline protease. |
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Stability & Cytotoxicity |
Peptide stability |
Literature report: |
The ACE inhibitory activity of the peptide was not affected by in vitro
incubation with gastrointestinal proteases (data not shown). This result
suggests that the purified peptide may be resistant to digestion in the
gastrointestinal tract. |
EHP-Tool: |
Enzymatic Hydrolysis Prediction Tool (EHP-Tool) |
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Peptide cytotoxicity |
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Additional information |
Additional information |
Smooth hound muscle is a promising protein source for the production of ACE inhibitory peptides that could be utilized to develop functional foods for prevention of hypertension. |
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Database cross-references |
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Reference(s) |
Primary literature |
Bougatef, A., Balti, R., Nedjar-Arroume, N., Ravallec, R., Adjé, E.Y., Souissi, N., et al. Evaluation of angiotensin I-converting enzyme (ACE) inhibitory activities of smooth hound (Mustelus mustelus) muscle protein hydrolysates generated by gastrointestinal proteases: identification of the most potent active peptide. European Food Research and Technology. 2010, 231, 127-35.
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Other literature(s) |
N.D |
PubDate |
2010 |
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