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 - DFBPANHY0120(Antihypertensive peptide)

DFBP ID	DFBPANHY0120
Peptide sequence	KVLPVPQ
Type	Native peptide
Peptide/Function name	Antihypertensive peptide

Function-activity relationship

Main bioactivity	Antihypertensive activity
Otheir bioactivity	ACE-inhibitory 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

N.D

pIC₅₀

N.D

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

Antihypertensive activity

Table 1. Effects of ACE Inhibitory Peptides on SBP of SHR
Sample	Dose (mg/kg)	Time after administration (hr)
Sample	Dose (mg/kg)	2	4	6	8	10
KVLPVPQ	1	―	―	-24.1 ± 7.8 *	―	―
KVLPVPQ	2	-20.2 ± 2.9	-26.3 ± 1.6	-31.5 ± 5.6 *	-25 ± 8.3	-22.7 ± 2.8
* Different from control (P < 0.05).

Specific target protein(s)

N.D

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

The potential for the antihypertensive peptide Lys-Val-Leu-Pro-Val-Pro-Gln in functional foods to mitigate hypertension would seem to merit further investigation.

Database cross-references

DFBP

[D1]	DFBPACEI0552
[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] Park Y W. Bioactive Components in Milk and Dairy Products[M]. 2009. [2] Ha, G.E., et al., Identification of Antihypertensive Peptides Derived from Low Molecular Weight Casein Hydrolysates Generated during Fermentation by Bifidobacterium longum KACC 91563. Korean Journal for Food Science of Animal Resources, 2015. 35(6): p. 738-747. [3] Fitzgerald R J, Murray B A, Walsh D J. Hypotensive peptides from milk proteins.[J]. Journal of Nutrition, 2004, 34(4):980S. [4] Bösze Z. Bioactive Components of Milk[M]. Springer New York, 2008. [5] Yamamoto, N., M. Ejiri, and S. Mizuno, Biogenic peptides and their potential use. Current Pharmaceutical Design, 2003. 9(16): p. 1345-1355.
PubDate	1996