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 - DFBPACEI0272(ACE-inhibitory peptide)

DFBP ID	DFBPACEI0272
Peptide sequence	AVPYPQR
Type	Native peptide
Peptide/Function name	ACE-inhibitory peptide, β-Casokinin-5, CEI_β7

Function-activity relationship

Main bioactivity	ACE-inhibitory activity
Otheir bioactivity	Antihypertensive activity ^[D1], Antioxidative activity ^[D2], Antithrombotic activity ^[D3], Multifunctional activity ^[D4]

Calculated physicochemical properties

Three-letter amino acid

Ala-Val-Pro-Tyr-Pro-Gln-Arg

Single-letter amino acid

AVPYPQR

Peptide length

Peptide mass

Experimental mass	Theoretical mass
N.D	829.95 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

9.82 ^c

IC₅₀

15.0 uM^[2-3], 274 uM ^[4]

pIC₅₀

-1.176, -2.438

GRAVY

-0.9286^c

Hydrophilic residue ratio

57.14%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Animal
Organism/Source	Milk protein
Precursor protein	β-Casein
Residue position	f(177-183)
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 potent Angiotensin-Converting Enzyme (ACE) (EC 3.4.15.1) inhibitory activity with an IC₅₀ value of 15.0 μM (274 μM ^[4]).
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(=O)N[C@@]([H])(C(C)C)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(Cc1ccc(O)cc1)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(CCC(=O)N)C(=O)N[C@@]([H])(CCCNC(=N)N)C(=O)O

Preparation method

Mode of preparation	Enzymatic hydrolysis
Enzyme(s)/starter culture	Bovine milk proteins were hydrolyzed with trypsin.

Stability & Cytotoxicity

Peptide stability

Literature report:	N.D
EHP-Tool:	Enzymatic Hydrolysis Prediction Tool (EHP-Tool)

Peptide cytotoxicity

Literature report:	No measured
Prediction:	ToxinPred

Additional information

The peptide was also found in fresh latex of the fig tree ^[D1].

Database cross-references

DFBP

[D1]	DFBPANHY0975
[D2]	DFBPANOX0126
[D3]	DFBPANTH0164
[D4]	DFBPMUFU0084

[D5]

[D6]

[D7]

[D8]

Reference(s)

Primary literature	Maruyama, S., Nakagomi, K., Tomizuka, N., Suzuki, H. Angiotensin I-Converting Enzyme Inhibitor Derived from an Enzymatic Hydrolysate of Casein. II. Isolation and Bradykinin-potentiating Activity on the Uterus and the Ileum of Rats. Agricultural and Biological Chemistry. 2014, 49, 1405-9. DOI: 10.1080/00021369.1985.10866901
Other literature(s)	[1] Park Y W. Bioactive Components in Milk and Dairy Products[M]. 2009. [2] Mizuno, S., & Yamamoto, N. (2004). Antihypertensive peptides from food proteins. Current Topics in Biotechnology, 1, 43–54. [3] Bösze Z. Bioactive Components of Milk[M]. Springer New York, 2008. [4] Pihlantoleppala A, Rokka T, Korhonen H. Angiotensin I converting enzyme inhibitory peptides derived from bovine milk proteins.[J]. International Dairy Journal, 1998, 8(8):325-331. [5] Maruyama, S., et al., Angiotensin I-Converting Enzyme-Inhibitors Derived from an Enzymatic Hydrolysate of Casein .4. Studies on the Active-Site and Antihypertensive Activity of Angiotensin I-Converting Enzyme-Inhibitors Derived from Casein. Agricultural and Biological Chemistry, 1987. 51(6): p. 1581-1586.
PubDate	2014