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 - DFBPACEI0713(ACE-inhibitory peptide)

DFBP ID	DFBPACEI0713
Peptide sequence	VRGPFPIIV
Type	Native peptide
Peptide/Function name	ACE-inhibitory peptide

Function-activity relationship

Main bioactivity	ACE-inhibitory activity
Otheir bioactivity	Antihypertensive activity ^[D1], Multifunctional activity ^[D2]

Calculated physicochemical properties

Three-letter amino acid

Val-Arg-Gly-Pro-Phe-Pro-Ile-Ile-Val

Single-letter amino acid

VRGPFPIIV

Peptide length

Peptide mass

Experimental mass	Theoretical mass
996.6 Da	997.24 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

11.04 ^c

IC₅₀

599 ± 55 uM

pIC₅₀

-2.777

GRAVY

1.3444^c

Hydrophilic residue ratio

88.89%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Animal
Organism/Source	Bovine milk protein
Precursor protein	β-Casein
Residue position	f(201-209)
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

ACE-inhibitory activity	The peptide exhibited low Angiotensin-Converting Enzyme (ACE) (EC 3.4.15.1) inhibitory activity with an IC₅₀ value of 599 ± 55 uM.
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])(C(C)C)C(=O)N[C@@]([H])(CCCNC(=N)N)C(=O)NCC(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(Cc1ccccc1)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])([C@]([H])(CC)C)C(=O)N[C@@]([H])([C@]([H])(CC)C)C(=O)N[C@@]([H])(C(C)C)C(=O)O

Preparation method

Mode of preparation	Fermentation
Enzyme(s)/starter culture	Milk was fermented with Enterococcus faecalis, CECT 5727.

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 potential of the peptide for use in functional foods to mitigate hypertension would seem to merit further clinical studies in humans.

Database cross-references

DFBP

[D1]	DFBPANHY0571
[D2]	DFBPMUFU0158

[D3]

[D4]

[D5]

[D6]

Reference(s)

Primary literature	Quirós, A., Ramos, M., Muguerza, B., Delgado, M.A., Miguel, M., Aleixandre, A., et al. Identification of novel antihypertensive peptides in milk fermented with Enterococcus faecalis. International Dairy Journal. 2007, 17, 33-41. DOI: 10.1016/j.idairyj.2005.12.011
Other literature(s)	[1] Miguel M, Recio I, Ramos M, et al. Antihypertensive effect of peptides obtained from Enterococcus faecalis-fermented milk in rats[J]. Journal of Dairy Science, 2006, 89(9):3352-3359. [2] Quirós A, Del M C M , Ramos M , et al. Stability to gastrointestinal enzymes and structure-activity relationship of beta-casein-peptides with antihypertensive properties.[J]. Peptides, 2009, 30(10):1848-1853. [3] Rojas-Ronquillo R , Cruz-Guerrero A , Angélica Flores-Nájera, et al. Antithrombotic and angiotensin-converting enzyme inhibitory properties of peptides released from bovine casein by Lactobacillus casei Shirota[J]. International Dairy Journal, 2012, 26(2).
PubDate	2007