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 - DFBPACEI0331(ACE-inhibitory peptide)

DFBP ID	DFBPACEI0331
Peptide sequence	FFVAPFPEVFGK
Type	Native peptide
Peptide/Function name	ACE-inhibitory peptide, CEI₁₂

Function-activity relationship

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

Calculated physicochemical properties

Three-letter amino acid

Phe-Phe-Val-Ala-Pro-Phe-Pro-Glu-Val-Phe-Gly-Lys

Single-letter amino acid

FFVAPFPEVFGK

Peptide length

Peptide mass

Experimental mass	Theoretical mass
N.D	1384.63 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

6.92 ^c

IC₅₀

18 uM

pIC₅₀

-1.255

GRAVY

0.8667^c

Hydrophilic residue ratio

83.33%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Animal
Organism/Source	Milk protein
Precursor protein	α_s1-Casein
Residue position	f(23-34) ^[6]
Precursor protein(s) search	Source.1: DFBPPR7717 ---- Milk proteins ---- Alpha-S1-casein Source.2: DFBPPR8488 ---- Milk proteins ---- Alpha-S1-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	(1) The peptide exhibited potent Angiotensin-Converting Enzyme (ACE) (EC 3.4.15.1) inhibitory activity with an IC₅₀ value of 18 μM. (2) ID₅₀ value (the concentration which inhibits 50% of the enzyme activity) of ACE inhibitor was calculated to be 77 μM ^[1,7]. (3) The peptide exhibited potent ACE-inhibitory activity with an IC₅₀ value of 108 μM ^[8].
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])(Cc1ccccc1)C(=O)N[C@@]([H])(Cc1ccccc1)C(=O)N[C@@]([H])(C(C)C)C(=O)N[C@@]([H])(C)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(Cc1ccccc1)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(CCC(=O)O)C(=O)N[C@@]([H])(C(C)C)C(=O)N[C@@]([H])(Cc1ccccc1)C(=O)NCC(=O)N[C@@]([H])(CCCCN)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:	N.D
Prediction:	ToxinPred

Additional information

(1) The use of a nisin as a ‘‘food-grade’’ inducer molecule, and generally-regarded-as-safe LAB species suggests that this system could be used for the production of functional food ingredients^[2].
(2) This peptide has the same structure as that reported for a bitter peptide ^[3].

Database cross-references

DFBP

[D1]	DFBPANHY0180, DFBPANHY0888
[D2]	DFBPANCA0110
[D3]	DFBPANTH0151
[D4]	DFBPMUFU0097

[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] Maruyama S , Suzuki H . A Peptide Inhibitor of Angiotensin I Converting Enzyme in the Tryptic Hydrolysate of Casein[J]. Journal of the Agricultural Chemical Society of Japan, 1982, 46(5):2. [2] Renye, J.A. and G.A. Somkuti, Nisin-induced expression of a recombinant antihypertensive peptide in dairy lactic acid bacteria. Biotechnology Letters, 2015. 37(7): p. 1447-1454. [3] Matoba T , Nagayasu C , Hayashi R , et al. Bitter Peptides in Tryptic Hydrolysate of Casein[J]. Agricultural and Biological Chemistry, 1969, 33(11):1662-1663. [4] Murray B A, Fitzgerald R J. Angiotensin converting enzyme inhibitory peptides derived from food proteins: biochemistry, bioactivity and production[J]. Current Pharmaceutical Design, 2007, 13(8):-. [5] Bösze Z. Bioactive Components of Milk[M]. Springer New York, 2008. [6] Tauzin, J., L. Miclo, and J.L. Gaillard, Angiotensin-I-converting enzyme inhibitory peptides from tryptic hydrolysate of bovine alphaS2-casein. FEBS Lett, 2002. 531(2): p. 369-74. [7] 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. [8] Paul, M., J.G. Phillips, and J.A. Renye, Jr., Short communication: Measuring the angiotensin-converting enzyme inhibitory activity of an 8-amino acid (8mer) fragment of the C12 antihypertensive peptide. J Dairy Sci, 2016. 99(5): p. 3263-3266. [9] De Oliveira, T.V., Polêto, M.D., De Oliveira, M.R., Silva, T.J., Barros, E., Guimarães, V.M., et al. Casein-Derived Peptides with Antihypertensive Potential: Production, Identification and Assessment of Complex Formation with Angiotensin I-Converting Enzyme (ACE) through Molecular Docking Studies. Food Biophysics. 2019, 15, 162-72.
PubDate	2014