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 - DFBPDPIV0096(DPP IV-inhibitory peptide)

DFBP ID	DFBPDPIV0096
Peptide sequence	VTGRFAGHPAAQ
Type	Native peptide
Peptide/Function name	DPP-IV inhibitory peptide, Anti-diabetic peptide

Function-activity relationship

Main bioactivity	DPP-IV and α-Glucosidase inhibitory activity
Otheir bioactivity	ACE-inhibitory activity ^[D1], Antioxidative activity ^[D2], α-Glucosidase inhibitory activity ^[D3], Multifunctional activity ^[D4]

Calculated physicochemical properties

Three-letter amino acid

Val-Thr-Gly-Arg-Phe-Ala-Gly-His-Pro-Ala-Ala-Gln

Single-letter amino acid

VTGRFAGHPAAQ

Peptide length

Peptide mass

Experimental mass	Theoretical mass
N.D	1211.34 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

11.04 ^c

IC₅₀

N.D

pIC₅₀

N.D

GRAVY

-0.1583^c

Hydrophilic residue ratio

66.67%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Animal
Organism/Source	Egg
Precursor protein	Egg yolk protein by-proudct
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 effective antidiabetic activity including α-glucosidase and Dipeptidyl Peptidase IV (EC 3.4.14.5) inhibitory with the IC₅₀ values of 365.4 μg/mL and 1402.2 μg/mL, respectively.
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])(C(C)C)C(=O)N[C@@]([H])([C@]([H])(O)C)C(=O)NCC(=O)N[C@@]([H])(CCCNC(=N)N)C(=O)N[C@@]([H])(Cc1ccccc1)C(=O)N[C@@]([H])(C)C(=O)NCC(=O)N[C@@]([H])(CC1=CN=C-N1)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(C)C(=O)N[C@@]([H])(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 following ethanol extraction of phospholipids was hydrolyzed with pepsin to produce and identify novel peptides.

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

Delipidated egg yolk proteins (YP) are the main by-products of lecithin extraction from egg yolk. The delipidation process, using ethanol and hexane for the removal of phospholipids, impairs protein functionality and so the YP possess limited biological and biotechnological value. YP by-products, however, can be converted into value-added products with functional and biological properties improved by enzymatic hydrolysis.

Database cross-references

DFBP

[D1]	DFBPACEI1772
[D2]	DFBPANOX0746
[D3]	DFBPALGL0029
[D4]	DFBPMUFU0553

BIOPEP-UWM

[D5]

8741, 8745, 8752

APD

[D6]

BioPepDB

[D7]

MBPDB

[D8]

Reference(s)

Primary literature	Zambrowicz A, Pokora M, Setner B, Dąbrowska A, Szołtysik M, Babij K, Szewczuk Z, Trziszka T, Lubec G, Chrzanowska J. Multifunctional peptides derived from an egg yolk protein hydrolysate: isolation and characterization. Amino Acids. 2015 Feb;47(2):369-80. PMID: 25408464 DOI: 10.1007/s00726-014-1869-x
Other literature(s)	N.D
PubDate	2015