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 - DFBPDPIV0127(DPP IV-inhibitory peptide)

DFBP ID	DFBPDPIV0127
Peptide sequence	EPPPPEPPPI
Type	Native peptide
Peptide/Function name	DPP-IV inhibitory peptide, Anti-diabetic peptide

Function-activity relationship

Main bioactivity	DPP-IV inhibitory activity
Otheir bioactivity	PEP-inhibitory activity ^[D1], Multifunctional activity ^[D2]

Calculated physicochemical properties

Three-letter amino acid

Glu-Pro-Pro-Pro-Pro-Glu-Pro-Pro-Pro-Ile

Single-letter amino acid

EPPPPEPPPI

Peptide length

Peptide mass

Experimental mass	Theoretical mass
N.D	1069.20 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

3.19 ^c

IC₅₀

N.D

pIC₅₀

N.D

GRAVY

-1.3700^c

Hydrophilic residue ratio

80%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Animal
Organism/Source	Bovine
Precursor protein	Brain protein
Residue position	N.D
Precursor protein(s) search	No matching precursor protein found
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	This peptide showed Dipeptidyl Peptidase IV (EC 3.4.14.5) inhibitory activity with the IC₅₀ values of 500 uM and it's weakly active.
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])(CCC(=O)O)C(=O)N1[C@@]([H])(CCC1)C(=O)N1[C@@]([H])(CCC1)C(=O)N1[C@@]([H])(CCC1)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(CCC(=O)O)C(=O)N1[C@@]([H])(CCC1)C(=O)N1[C@@]([H])(CCC1)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])([C@]([H])(CC)C)C(=O)O

Preparation method

Mode of preparation	Chemical synthesis
Enzyme(s)/starter culture	The peptide was synthesized by the solid phase method with a 430A Peptide Synthesizer (Applied Biosystems. Inc.).

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]	DFBPPEPI0089
[D2]	DFBPMUFU0732

[D3]

[D4]

[D5]

[D6]

Reference(s)

Primary literature	Maruyama S, Ohmori T, Nakagami T. Prolylendopeptidase inhibitory activity of a glial fibrillary acidic protein fragment and other proline-rich peptides. Biosci Biotechnol Biochem. 1996 Feb;60(2):358-9. PMID: 9063991 DOI: 10.1271/bbb.60.358
Other literature(s)	[1] Ohmori T, Nakagami T, Tanaka H, et al. Isolation of prolylendopeptidase-inhibiting peptides from bovine brain.[J]. Biochemical & Biophysical Research Communications, 1994, 202(2):809. [2] Lacroix, I.M.E., Li-Chan, E.C.Y. Evaluation of the potential of dietary proteins as precursors of dipeptidyl peptidase (DPP)-IV inhibitors by an in silico approach. Journal of Functional Foods. 2012, 4, 403-22.
PubDate	1996