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 - DFBPPEPI0089(PEP-inhibitory peptide)

DFBP ID	DFBPPEPI0089
Peptide sequence	EPPPPEPPPI
Type	Native peptide
Peptide/Function name	PEP-inhibitory peptide

Function-activity relationship

Main bioactivity	PEP-inhibitory activity
Otheir bioactivity	DPP IV-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
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

PEP-inhibitory activity

The peptide showed low inhibitory activity against Prolyl endopeptidase (EC:3.4.21.26) with the IC₅₀ and K_i values of 634 and 1400 uM, respectively.

Table 1 PEP inhibitory activity of synthetic peptides
Peptide	IC₅₀ (μM)	K_i (μM)
EPPPPEPPPI	634	1400

Specific target protein(s)

Specific Target Protein(s):
Prolyl endopeptidase

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	Chmical 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]	DFBPDPIV0127
[D2]	DFBPMUFU0732

[D3]

[D4]

[D5]

[D6]

Reference(s)

Primary literature	Ohmori T, Nakagami T, Tanaka H, Maruyama S. Isolation of prolylendopeptidase-inhibiting peptides from bovine brain. Biochem Biophys Res Commun. 1994 Jul 29;202(2):809-15. PMID: 8048952 DOI: 10.1006/bbrc.1994.2002
Other literature(s)	N.D
PubDate	1994