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 - DFBPACEI0552(ACE-inhibitory peptide)

DFBP ID	DFBPACEI0552
Peptide sequence	KVLPVPQ
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

Lys-Val-Leu-Pro-Val-Pro-Gln

Single-letter amino acid

KVLPVPQ

Peptide length

Peptide mass

Experimental mass	Theoretical mass
N.D	779.98 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

10.04 ^c

IC₅₀

1000 uM

pIC₅₀

-3.0

GRAVY

0.2286^c

Hydrophilic residue ratio

71.43%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Animal
Organism/Source	Milk protein
Precursor protein	β-Casein
Residue position	f(169-175)
Precursor protein(s) search	Source.1: DFBPPR7665 ---- Milk proteins ---- Beta-casein Source.2: DFBPPR7692 ---- Milk proteins ---- Beta-casein Source.3: DFBPPR7700 ---- Milk proteins ---- Beta-casein Source.4: DFBPPR7718 ---- Milk proteins ---- Beta-casein Source.5: 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 1000 μM.
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])(CCCCN)C(=O)N[C@@]([H])(C(C)C)C(=O)N[C@@]([H])(CC(C)C)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(C(C)C)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(CCC(=O)N)C(=O)O

Preparation method

Mode of preparation	Enzymatic hydrolysis
Enzyme(s)/starter culture	Milk proteins were hydrolyzed by an extracellular proteinase from Lactobacillus helveticus CP790.

Stability & Cytotoxicity

Peptide stability

Literature report:	The peptide was incubated with gastrointestinal enzymes (pepsin, pancreatin, and carboxypeptidase A) and the short peptide KVLPVP was released.
EHP-Tool:	Enzymatic Hydrolysis Prediction Tool (EHP-Tool)

Peptide cytotoxicity

Literature report:	Non-Toxin
Prediction:	ToxinPred

Additional information

N.D

Database cross-references

DFBP

[D1]	DFBPANHY0120
[D2]	DFBPMUFU0133

[D3]

[D4]

[D5]

[D6]

Reference(s)

Primary literature	Maeno, M., Yamamoto, N., Takano, T. Identification of an Antihypertensive Peptide from Casein Hydrolysate Produced by a Proteinase from Lactobacillus helveticus CP790. Journal of Dairy Science. 1996, 79, 1316-21. DOI: 10.3168/jds.S0022-0302(96)76487-1
Other literature(s)	[1] Robert, M.C., et al., Identification of angiotensin-I-converting enzyme inhibitory peptides derived from sodium caseinate hydrolysates produced by Lactobacillus helveticus NCC 2765. J Agric Food Chem, 2004. 52(23): p. 6923-31.
PubDate	1996