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 - DFBPACEI0273(ACE-inhibitory peptide)

DFBP ID	DFBPACEI0273
Peptide sequence	YQQPVLGPVR
Type	Native peptide
Peptide/Function name	ACE-inhibitory peptide, β-Casokinin-10

Function-activity relationship

Main bioactivity	ACE-inhibitory activity
Otheir bioactivity	Immunomodulatory activity ^[D1], Multifunctional activity ^[D2]

Calculated physicochemical properties

Three-letter amino acid

Tyr-Gln-Gln-Pro-Val-Leu-Gly-Pro-Val-Arg

Single-letter amino acid

YQQPVLGPVR

Peptide length

Peptide mass

Experimental mass	Theoretical mass
N.D	1156.35 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

9.82 ^c

IC₅₀

300 uM ^[2-3]

pIC₅₀

-2.477

GRAVY

-0.4200^c

Hydrophilic residue ratio

60%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Animal
Organism/Source	Bovine milk protein
Precursor protein	β-Casein
Residue position	f(193-202)
Precursor protein(s) search	No matching precursor protein found
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 moderate Angiotensin-Converting Enzyme (ACE) (EC 3.4.15.1) inhibitory activity with an IC₅₀ value of 300 uM ^[2-3].
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])(Cc1ccc(O)cc1)C(=O)N[C@@]([H])(CCC(=O)N)C(=O)N[C@@]([H])(CCC(=O)N)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(C(C)C)C(=O)N[C@@]([H])(CC(C)C)C(=O)NCC(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(C(C)C)C(=O)N[C@@]([H])(CCCNC(=N)N)C(=O)O

Preparation method

Mode of preparation	Synthesis, Enzymatic hydrolysis^[2,3].
Enzyme(s)/starter culture	Hydrolysis with Proteinase ^[2,3].

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

N.D

Database cross-references

DFBP

[D1]	DFBPIMMU0027
[D2]	DFBPMUFU0085

[D3]

[D4]

[D5]

[D6]

Reference(s)

Primary literature	Meisel, H., Schlimme, E. Inhibitors of angiotensin-converting-enzyme derived from bovine casein (casokinins). β-Casomorphins and Related Peptides: Recent Developments. 1994, 27-33.
Other literature(s)	[1] Park Y W. Bioactive Components in Milk and Dairy Products[M]. 2009. [2] Saito T, Nakamura T, Kitazawa H, et al. Isolation and structural analysis of antihypertensive peptides that exist naturally in Gouda cheese[J]. Journal of Dairy Science, 2000, 83(7):1434-40. [3] Bösze Z. Bioactive Components of Milk[M]. Springer New York, 2008. [4] Casokinins as bioactive peptides in the primary strucure of casein. In: Food proteins, structure and functionality ed Schwenke K.D., Mothes R., VCh, Weinheim - New York - Basel - Cambridge - Tokyo, pp 67-75.
PubDate	1994