Peptide properties

1Top 2Function-activity relationship 3Calculated physicochemical properties 4Peptide source & Food-borne protein(s) search 5Biological/Functional activity & target protein 6Taste properties & Structure 7Preparation method 8Stability & Cytotoxicity 9Additional information 10Database cross-references 11Reference(s)

List of peptide properties

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

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	Source.1: DFBPPR10297 ---- Animal proteins ---- Vitellogenin-2
Link-research Inductive analysis	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

Structure

Embedded Mol* Viewer

Docking

Embedded Mol* Viewer

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

Literature report:	N.D
EHP-Tool:	Enzymatic Hydrolysis Prediction Tool (EHP-Tool)

Peptide cytotoxicity

Literature report:	N.D
Prediction:	ToxinPred

Additional information

N.D

Database cross-references

DFBP

[D1]	DFBPACEI1861
[D2]	DFBPANOX0455
[D3]	DFBPMUFU0570

BIOPEP-UWM

[D4]

8387, 8552, 8553

APD

[D5]

BioPepDB

[D6]

MBPDB

[D7]

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. DOI: 10.1039/c4ra12943a
Other literature(s)	N.D
PubDate	2015