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 - DFBPACEI1466(ACE-inhibitory peptide)

DFBP ID	DFBPACEI1466
Peptide sequence	HPHPHLSF
Type	Native peptide
Peptide/Function name	ACE-inhibitory peptide

Function-activity relationship

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

Calculated physicochemical properties

Three-letter amino acid

His-Pro-His-Pro-His-Leu-Ser-Phe

Single-letter amino acid

HPHPHLSF

Peptide length

Peptide mass

Experimental mass	Theoretical mass
970.3 Da	971.08 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

8.04 ^c

IC₅₀

28.9 uM

pIC₅₀

-1.461

GRAVY

-0.8750^c

Hydrophilic residue ratio

50%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Animal
Organism/Source	Ovine milk protein
Precursor protein	κ-Casein
Residue position	f(98-105)
Precursor protein(s) search	Source.1: DFBPPR7686 ---- Milk proteins ---- Kappa-casein Source.2: DFBPPR7695 ---- Milk proteins ---- Kappa-casein Source.3: DFBPPR7715 ---- Milk proteins ---- Kappa-casein Source.4: DFBPPR8492 ---- Milk proteins ---- Kappa-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 28.9 μM.
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])(CC1=CN=C-N1)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(CC1=CN=C-N1)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(CC1=CN=C-N1)C(=O)N[C@@]([H])(CC(C)C)C(=O)N[C@@]([H])(CO)C(=O)N[C@@]([H])(Cc1ccccc1)C(=O)O

Preparation method

Mode of preparation	Enzymatic hydrolysis
Enzyme(s)/starter culture	Enzymatic hydrolysis of ovine milk was performed by using proteolytic enzymes of gastrointestinal origin. The most active hydrolysate, corresponding to κ-casein hydrolyzed with pepsin, chymotrypsin, and 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

The peptide showed ACEI activities lower than 30 μM, making it a good candidate to be used as antihypertensive agent in functional products.

Database cross-references

DFBP

[D1]	DFBPANHY0968
[D2]	DFBPANOX0258
[D3]	DFBPMUFU0397

[D4]

[D5]

[D6]

[D7]

Reference(s)

Primary literature	Gómez-Ruiz JA, Ramos M, Recio I. Identification of novel angiotensin-converting enzyme-inhibitory peptides from ovine milk proteins by CE-MS and chromatographic techniques. Electrophoresis. 2007 Nov;28(22):4202-11. PMID: 17948260 DOI: 10.1002/elps.200700324
Other literature(s)	N.D
PubDate	2007