| DFBP ID - DFBPDPIV0032(DPP IV-inhibitory peptide) |
| DFBP ID |
DFBPDPIV0032 |
| Peptide sequence |
RNDDLNYIQ |
| Type |
Native peptide |
| Peptide/Function name |
DPP-IV inhibitory peptide, Anti-diabetic peptide |
|
| Function-activity relationship |
| Main bioactivity |
DPP-IV inhibitory activity |
| Otheir bioactivity |
ACE-inhibitory activity [D1], Antioxidative activity [D2], Multifunctional activity [D3] |
|
| Calculated physicochemical properties |
| Three-letter amino acid |
Arg-Asn-Asp-Asp-Leu-Asn-Tyr-Ile-Gln |
| Single-letter amino acid |
RNDDLNYIQ |
| Peptide length |
9 |
| Peptide mass |
| Experimental mass |
Theoretical mass |
| N.D |
1150.20 Da c |
|
| Net charge |
0.00 c |
| Isoelectric point (pI) |
3.92 c |
| IC50 |
N.D |
| pIC50 |
N.D |
| GRAVY |
-1.6667 c |
| Hydrophilic residue ratio |
22.22% c |
| Peptide calculator |
|
|
| Peptide source & Food-borne protein(s) search |
| Classification |
Animal |
| Organism/Source |
Egg |
| Precursor protein |
Egg-yolk protein by-product |
| Residue position |
N.D |
|
Precursor protein(s) search
|
|
|
Link-research
|
There are no literature reports on the discovery of this sequence in other food-source proteins. |
|
| Biological/Functional activity & target protein |
| DPP IV-inhibitory activity |
The peptide showed Dipeptidyl Peptidase IV (EC 3.4.14.5) inhibitory activity with the IC50 values between 361.5 and 426.25 μmol/L (data not shown). This peptide had no inhibiton for α-glucosidase. |
| Specific target protein(s) |
Specific Target Protein(s):
Dipeptidyl peptidase 4 |
|
| Taste properties & Structure |
| Bitterness |
| Literature report |
N.D |
| Bitter prediction tools |
Non-bitter taste prediction |
|
| SMILES |
N[C@@]([H])(CCCNC(=N)N)C(=O)N[C@@]([H])(CC(=O)N)C(=O)N[C@@]([H])(CC(=O)O)C(=O)N[C@@]([H])(CC(=O)O)C(=O)N[C@@]([H])(CC(C)C)C(=O)N[C@@]([H])(CC(=O)N)C(=O)N[C@@]([H])(Cc1ccc(O)cc1)C(=O)N[C@@]([H])([C@]([H])(CC)C)C(=O)N[C@@]([H])(CCC(=O)N)C(=O)O |
|
| Preparation method |
| Mode of preparation |
Enzymatic hydrolysis |
| Enzyme(s)/starter culture |
The egg-yolk protein by-product was prepared with a proteinase from Asian pumpkin (Cucurbita ficifolia). |
|
| Stability & Cytotoxicity |
| Peptide stability |
|
| Peptide cytotoxicity |
|
|
| Additional information |
| Additional information |
N.D |
|
| Database cross-references |
|
|
|
|
|
|
|
|
|
|
| Reference(s) |
| Primary literature |
Zambrowicz, A., Eckert, E., Pokora, M., Bobak, Ł., Dąbrowska, A., Szołtysik, M., et al. Antioxidant and antidiabetic activities of peptides isolated from a hydrolysate of an egg-yolk protein by-product prepared with a proteinase from Asian pumpkin (Cucurbita ficifolia). RSC Advances. 2015, 5, 10460-7.
|
| Other literature(s) |
N.D |
| PubDate |
2015 |
|
