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 - DFBPANHY0550(Antihypertensive peptide)

DFBP ID	DFBPANHY0550
Peptide sequence	VYPFPG
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

Val-Tyr-Pro-Phe-Pro-Gly

Single-letter amino acid

VYPFPG

Peptide length

Peptide mass

Experimental mass	Theoretical mass
678.86 Da	678.78 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

5.92 ^c

IC₅₀

N.D

pIC₅₀

N.D

GRAVY

0.3500^c

Hydrophilic residue ratio

83.33%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Animal
Organism/Source	Milk protein
Precursor protein	β-Casein
Residue position	f(59-64)
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

Antihypertensive activity

Table 1 The antihypertensive activity of synthetic peptide.
Peptide	In vitro experiments	Dose (mg/kg)	SBP (mm Hg) ¹
			Mean	SE
VYPFPG	SHR	8.0	-22.0*	4.6
¹ Systolic blood pressure; changes in SBP of SHR at 6 h after a gastric intubation. Values are means of three determinations. * Different from the 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])(C(C)C)C(=O)N[C@@]([H])(Cc1ccc(O)cc1)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(Cc1ccccc1)C(=O)N1[C@@]([H])(CCC1)C(=O)NCC(=O)O

Preparation method

Mode of preparation	Enzymatic hydrolysis
Enzyme(s)/starter culture	Whey protein was digested with Proteinase K at 37 ℃ for 24 h.

Stability & Cytotoxicity

Peptide stability

Literature report:	N.D
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]	DFBPACEI0343
[D2]	DFBPMUFU0102

[D3]

[D4]

[D5]

[D6]

Reference(s)

Primary literature	Abubakar, A., Saito, T., Kitazawa, H., Kawai, Y., Itoh, T. Structural analysis of new antihypertensive peptides derived from cheese whey protein by proteinase K digestion. J Dairy Sci. 1998, 81, 3131-8. DOI: 10.3168/jds.S0022-0302(98)75878-3
Other literature(s)	[1] Yamamoto N, Ejiri M, Mizuno S. Biogenic peptides and their potential use[J]. Curr Pharm Des, 2003, 9(16):-. [2] ZsuzsannaBösze. Bioactive Components of Milk[M]. Springer New York, 2008. [3] Martinez-Maqueda, D., et al., Antihypertensive peptides from food proteins: a review. Food Funct, 2012. 3(4): p. 350-361.
PubDate	1998