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 - DFBPANOX0258(Antioxidative peptide)

DFBP ID	DFBPANOX0258
Peptide sequence	HPHPHLSF
Type	Native peptide
Peptide/Function name	Antioxidative peptide

Function-activity relationship

Main bioactivity	Antioxidative activity
Otheir bioactivity	ACE-inhibitory activity ^[D1], Antihypertensive 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
970.4 Da	971.08 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

8.04 ^c

IC₅₀

N.D

pIC₅₀

N.D

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

Antioxidative activity

(1) The peptide HPHPHLSF was a potent inhibitor of linoleic acid oxidation with an activity similar to that obtained with the synthetic antioxidant BHT at a range of concentrations from 1,000 to 1μM. As an example, 1μM concentration of HPHPHLSF at the third day of assay had an antioxidant percentage of 74.1%, and the same concentration of BHT displayed an antioxidant percentage of 88.4%.
(2) The antioxidant activity of the peptide was dose-dependant. At the third day of assay the highest concentration of peptide revealed an antioxidant activity of 43.7%, considerably lower than when the concentration was diminished 10³ times, for which an activity of 74.1% was measured.

Specific target protein(s)

N.D

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	Ovine casein proteins were hydrolyzed with gastrointestinal enzymes including pepsin, trypsin and chymotrypsin.

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

Ovine caseins could be considered as suitable natural antioxidants to prevent oxidation reactions in food processing and become ingredients of functional foods.

Database cross-references

DFBP

[D1]	DFBPACEI1466
[D2]	DFBPANHY0968
[D3]	DFBPMUFU0397

[D4]

[D5]

[D6]

[D7]

Reference(s)

Primary literature	Gómez-Ruiz, J.Á., López-Expósito, I., Pihlanto, A., Ramos, M., Recio, I. Antioxidant activity of ovine casein hydrolysates: identification of active peptides by HPLC–MS/MS. European Food Research and Technology. 2008, 227, 1061-7. DOI: 10.1007/s00217-008-0820-3
Other literature(s)	[1] Park Y W. Bioactive Components in Milk and Dairy Products[M]. 2009.
PubDate	2008