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 - DFBPACEI1462(ACE-inhibitory peptide)

DFBP ID	DFBPACEI1462
Peptide sequence	YQEPVLGP
Type	Native peptide
Peptide/Function name	ACE-inhibitory peptide

Function-activity relationship

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

Calculated physicochemical properties

Three-letter amino acid

Tyr-Gln-Glu-Pro-Val-Leu-Gly-Pro

Single-letter amino acid

YQEPVLGP

Peptide length

Peptide mass

Experimental mass	Theoretical mass
N.D	902.01 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

3.34 ^c

IC₅₀

653.98 ± 0.22 ug/mL

pIC₅₀

-2.816

GRAVY

-0.4875^c

Hydrophilic residue ratio

62.5%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Animal
Organism/Source	Caprine milk
Precursor protein	β-Casein
Residue position	f(191-198)
Precursor protein(s) search	Source.1: DFBPPR7692 ---- Milk proteins ---- Beta-casein Source.2: DFBPPR7700 ---- Milk proteins ---- Beta-casein Source.3: DFBPPR7718 ---- Milk proteins ---- Beta-casein Source.4: DFBPPR8489 ---- Milk proteins ---- Beta-casein
Link-research Inductive analysis	Link 1: DFBPACEI1461----Ovine milk----β-Casein

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 653.98 ± 0.22 ug/mL.
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)O)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)O

Preparation method

Mode of preparation	Enzymatic hydrolysis
Enzyme(s)/starter culture	Hydrolysis with Cheeselike system (Raw and sterilized caprine cheeselike systems, manufactured with proteases from C. cardunculus, are a source of peptides with ACE-inhibitory and antioxidant activities.).

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

(1) Despite their moderate bioactivity, they intrinsically behave as functional foods, so they may eventually be recommended for inclusion in one’s daily diet as a more appealing, health-promoting vector than the direct use of more potent drugs.
(2) In the Iberian Peninsula, several raw ovine and caprine milk cheeses have been manufactured on the farm level since ancient times. Extract of the flowers of Cynara cardunculus have been used as the coagulant.

Database cross-references

DFBP

[D1]	DFBPANOX0691, DFBPANOX0692
[D2]	DFBPMUFU0395

[D3]

[D4]

[D5]

[D6]

Reference(s)

Primary literature	Silva SV, Pihlanto A, Malcata FX. Bioactive peptides in ovine and caprine cheeselike systems prepared with proteases from Cynara cardunculus. J Dairy Sci. 2006 Sep;89(9):3336-44. PMID: 16899666 DOI: 10.3168/jds.S0022-0302(06)72370-0
Other literature(s)	N.D
PubDate	2006