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 - DFBPPEPI0095(PEP-inhibitory peptide)

DFBP ID	DFBPPEPI0095
Peptide sequence	AVPYPQRDMPIQAFLLY
Type	Native peptide
Peptide/Function name	PEP-inhibitory peptide

Function-activity relationship

Main bioactivity	PEP-inhibitory activity
Otheir bioactivity	N.D

Calculated physicochemical properties

Three-letter amino acid

Ala-Val-Pro-Tyr-Pro-Gln-Arg-Asp-Met-Pro-Ile-Gln-Ala-Phe-Leu-Leu-Tyr

Single-letter amino acid

AVPYPQRDMPIQAFLLY

Peptide length

Peptide mass

Experimental mass	Theoretical mass
1714.02 Da	2022.37 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

6.62 ^c

IC₅₀

N.D

pIC₅₀

N.D

GRAVY

0.1294^c

Hydrophilic residue ratio

64.71%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Animal
Organism/Source	Sodium caseinate (from cow milk)
Precursor protein	β-Casein
Residue position	N.D
Precursor protein(s) search	Source.1: DFBPPR7718 ---- Milk proteins ---- Beta-casein Source.2: DFBPPR8489 ---- Milk proteins ---- Beta-casein
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 AVPYPQRDMPIQAFLLY exhibited potent Prolyl endopeptidase (PEP) (EC:3.4.21.26) inhibitory activity with an IC₅₀ value of 48.2 uM (positive control: Bacitracin IC₅₀ = 124.6 uM), and its PEP-inhibitory pattern was shown by Lineweaver–Burk plots to be a competitive inhibition pattern.
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])(C)C(=O)N[C@@]([H])(C(C)C)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(Cc1ccc(O)cc1)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(CCC(=O)N)C(=O)N[C@@]([H])(CCCNC(=N)N)C(=O)N[C@@]([H])(CC(=O)O)C(=O)N[C@@]([H])(CCSC)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])([C@]([H])(CC)C)C(=O)N[C@@]([H])(CCC(=O)N)C(=O)N[C@@]([H])(C)C(=O)N[C@@]([H])(Cc1ccccc1)C(=O)N[C@@]([H])(CC(C)C)C(=O)N[C@@]([H])(CC(C)C)C(=O)N[C@@]([H])(Cc1ccc(O)cc1)C(=O)O

Preparation method

Mode of preparation	Enzymatic hydrolysis
Enzyme(s)/starter culture	The hydrolysate obtained from sodium caseinate using bromelain (SC/BML) displayed the highest inhibitory activity of 86.8% at 5 mg/mL in the present study, and its IC₅₀ value against PEP was 0.77 mg/mL.

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

This study indicates that sodium caseinate has the potential to be the source of the functional food for prevention of neurological disorders.

Database cross-references

[D1]

[D2]

[D3]

[D4]

Reference(s)

Primary literature	Hsieh CH, Wang TY, Hung CC, Hsieh YL, Hsu KC. Isolation of prolyl endopeptidase inhibitory peptides from a sodium caseinate hydrolysate. Food Funct. 2016 Jan;7(1):565-73. PMID: 26574880 DOI: 10.1039/c5fo01262g
Other literature(s)	N.D
PubDate	2016