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 - DFBPDPIV0031(DPP IV-inhibitory peptide)

DFBP ID	DFBPDPIV0031
Peptide sequence	LAPSLPGKPKPD
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], α-Glucosidase inhibitory activity ^[D3], Multifunctional activity ^[D4]

Calculated physicochemical properties

Three-letter amino acid

Leu-Ala-Pro-Ser-Leu-Pro-Gly-Lys-Pro-Lys-Pro-Asp

Single-letter amino acid

LAPSLPGKPKPD

Peptide length

Peptide mass

Experimental mass	Theoretical mass
N.D	1219.42 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

9.84 ^c

IC₅₀

N.D

pIC₅₀

N.D

GRAVY

-0.7917^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-product
Residue position	N.D
Precursor protein(s) search	Source.1: DFBPPR10968 ---- Animal proteins ---- Visual system homeobox 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 of 361.5 μmol/L and it also exerted α-glucosidase inhibitory activity with the IC₅₀ values of 1065.6 μmol/L.
Specific target protein(s)	Specific Target Protein(s): Dipeptidyl peptidase 4

Taste properties & Structure

Bitterness

Literature report	N.D
Bitter prediction tools	Bitter taste ^prediction

SMILES

N[C@@]([H])(CC(C)C)C(=O)N[C@@]([H])(C)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(CO)C(=O)N[C@@]([H])(CC(C)C)C(=O)N1[C@@]([H])(CCC1)C(=O)NCC(=O)N[C@@]([H])(CCCCN)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(CCCCN)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(CC(=O)O)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

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

Peptide cytotoxicity

Literature report:	N.D
Prediction:	ToxinPred

Additional information

The results showed that peptide: LAPSLPGKPKPD obtained in this study showed much lower DPP-IV inhibitory activity than other reported peptides, which may be determined by the peptide length.

Database cross-references

DFBP

[D1]	DFBPACEI1862
[D2]	DFBPANOX0390
[D3]	DFBPALGL0020
[D4]	DFBPMUFU0571

BIOPEP-UWM

[D5]

8388, 8547, 8548, 8550

APD

[D6]

BioPepDB

[D7]

MBPDB

[D8]

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)	[1] Eckert E, Zambrowicz A, Pokora M, et al. Egg-yolk protein by-product as a source of ACE-inhibitory peptides obtained with using unconventional proteinase from Asian pumpkin (Cucurbita ficifolia)[J]. Journal of Proteomics, 2014, 110:107-116.
PubDate	2015