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 - DFBPACEI0083(ACE-inhibitory peptide)

DFBP ID	DFBPACEI0083
Peptide sequence	YPVQPFTE
Type	Native peptide
Peptide/Function name	ACE-inhibitory peptide

Function-activity relationship

Main bioactivity	ACE-inhibitory activity
Otheir bioactivity	Vasoconstriction activity ^[D1], Opioid activity ^[D2], Multifunctional activity ^[D3]

Calculated physicochemical properties

Three-letter amino acid

Tyr-Pro-Val-Gln-Pro-Phe-Thr-Glu

Single-letter amino acid

YPVQPFTE

Peptide length

Peptide mass

Experimental mass	Theoretical mass
N.D	980.08 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

3.34 ^c

IC₅₀

0.00034 M (0.37 mg/ml)

pIC₅₀

3.469

GRAVY

-0.6500^c

Hydrophilic residue ratio

50%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Animal
Organism/Source	Bovine whey protein
Precursor protein	γ-Casein
Residue position	f(114-121)
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

ACE-inhibitory activity	The peptide exhibited potent Angiotensin-Converting Enzyme (ACE) (EC 3.4.15.1) inhibitory activity with an IC₅₀ value of 0.00034 M (0.37 mg/ml), and its ACE inhibitory pattern was shown by Lineweaver–Burk plots to be a competitive inhibition pattern.
Specific target protein(s)	Specific Target Protein(s): Angiotensin-converting enzyme

Taste properties & Structure

Bitterness

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

SMILES

N[C@@]([H])(Cc1ccc(O)cc1)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(C(C)C)C(=O)N[C@@]([H])(CCC(=O)N)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(Cc1ccccc1)C(=O)N[C@@]([H])([C@]([H])(O)C)C(=O)N[C@@]([H])(CCC(=O)O)C(=O)O

Preparation method

Mode of preparation	Enzymatic hydrolysis
Enzyme(s)/starter culture	γ-Casein (4.0 g) was incubated with 40 mg of trypsin-TPCK in 0.02 M ammonium bicarbonate, pH 8.0, at 37 ℃ for 15 min. The incubation was stopped by heating for 3 min in boiling water.

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 traditional product (probiotic sheep milk yoghurt) may possess multifunctional health effects, due to the presence of probiotics and bioac- tive peptides.

Database cross-references

DFBP

[D1]	DFBPVACO0003
[D2]	DFBPOPIO0076
[D3]	DFBPMUFU0041

[D4]

[D5]

[D6]

[D7]

Reference(s)

Primary literature	Lebrun I, Lebrun FL, Henriques OB, Carmona AK, Juliano L, Camargo AC. Isolation and characterization of a new bradykinin potentiating octapeptide from gamma-casein. Can J Physiol Pharmacol. 1995 Jan;73(1):85-91. PMID: 7600458 DOI: 10.1139/y95-012
Other literature(s)	[1] Papadimitriou C G, Vafopoulou-Mastrojiannaki A, Silva S V, et al. Identification of peptides in traditional and probiotic sheep milk yoghurt with angiotensin I-converting enzyme (ACE)-inhibitory activity[J]. Food Chemistry, 2007, 105(2):647-656. [2] Perpetuo E A, Juliano L, Lebrun I. Biochemical and pharmacological aspects of two bradykinin-potentiating peptides obtained from tryptic hydrolysis of casein.[J]. J Protein Chem, 2003, 22(7-8):601-606.
PubDate	1995