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 - DFBPANHY0575(Antihypertensive peptide)

DFBP ID	DFBPANHY0575
Peptide sequence	YPFPGPIPN
Type	Native peptide
Peptide/Function name	Antihypertensive peptide

Function-activity relationship

Main bioactivity	Antihypertensive activity
Otheir bioactivity	ACE-inhibitory activity ^[D1], DPP IV-inhibitory activity ^[D2], Opioid activity ^[D3], Multifunctional activity ^[D4]

Calculated physicochemical properties

Three-letter amino acid

Tyr-Pro-Phe-Pro-Gly-Pro-Ile-Pro-Asn

Single-letter amino acid

YPFPGPIPN

Peptide length

Peptide mass

Experimental mass	Theoretical mass
1001 Da	1001.14 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

5.92 ^c

IC₅₀

N.D

pIC₅₀

N.D

GRAVY

-0.4778^c

Hydrophilic residue ratio

77.78%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Animal
Organism/Source	Milk protein, Gouda Cheese (8 months)
Precursor protein	β-Casein
Residue position	f(60-68)
Precursor protein(s) search	Source.1: 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	The peptide did not have strong antihypertensive activity and the antihypertensive effects on SHR was -7.0 ± 3.8 mm Hg at a dose of 7.5 mg/kg.
Specific target protein(s)	N.D

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])(Cc1ccccc1)C(=O)N1[C@@]([H])(CCC1)C(=O)NCC(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])([C@]([H])(CC)C)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(CC(=O)N)C(=O)O

Preparation method

Mode of preparation	Preparation of water-soluble peptides from ripened-type cheeses
Enzyme(s)/starter culture	The water-soluble peptides of Gouda cheese (8 months) were fractionated by hydrophobic chromatography with stepwise elution from 15 to 90% (vol/vol) CH₃OH (at 15% intervals).

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]	DFBPACEI0662, DFBPACEI1470
[D2]	DFBPDPIV0072
[D3]	DFBPOPIO0144
[D4]	DFBPMUFU0146

[D5]

[D6]

[D7]

[D8]

Reference(s)

Primary literature	Saito, T., Nakamura, T., Kitazawa, H., Kawai, Y., Itoh, T. Isolation and Structural Analysis of Antihypertensive Peptides That Exist Naturally in Gouda Cheese. Journal of Dairy Science. 2000, 83, 1434-40. DOI: 10.3168/jds.S0022-0302(00)75013-2
Other literature(s)	[1] Park Y W. Bioactive Components in Milk and Dairy Products[M]. 2009. [2] Huth P J, Dirienzo D B, Miller G D. Major scientific advances with dairy foods in nutrition and health[J]. Journal of Dairy Science, 2006, 89(4):1207-1221. [3] ZsuzsannaBösze. Bioactive Components of Milk[M]. Springer New York, 2008. [4] Martinez-Maqueda, D., et al., Antihypertensive peptides from food proteins: a review. Food Funct, 2012. 3(4): p. 350-361.
PubDate	2000