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 - DFBPANOX0004(Antioxidative peptide)

DFBP ID	DFBPANOX0004
Peptide sequence	LLPHHADADY
Type	Native peptide
Peptide/Function name	Antioxidative peptide, P4

Function-activity relationship

Main bioactivity	Antioxidative activity
Otheir bioactivity	N.D

Calculated physicochemical properties

Three-letter amino acid

Leu-Leu-Pro-His-His-Ala-Asp-Ala-Asp-Tyr

Single-letter amino acid

LLPHHADADY

Peptide length

Peptide mass

Experimental mass	Theoretical mass
1151.9 Da	1151.22 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

4.96 ^c

IC₅₀

N.D

pIC₅₀

N.D

GRAVY

-0.5100^c

Hydrophilic residue ratio

50%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Plant
Organism/Source	Soybean protein
Precursor protein	β-Conglycinin (7S protein)
Residue position	N.D
Precursor protein(s) search	Source.1: DFBPPR4990 ---- Plant proteins ---- Beta-conglycinin alpha' subunit
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	This peptide yielded antioxidative activity against the peroxidation of linoleic acid in an aqueous system at pH 7.0. The antioxidative activity was measured with 69 μg of P4 and the peptide concentrations ranged from 3.3 × 10^-7 to 4.5 × 10^-5 M, in which range the antioxidative activity was dose dependent and no prooxidative activity was observed (data not shown).
Specific target protein(s)	N.D

Taste properties & Structure

Bitterness

Literature report	N.D
Bitter prediction tools	No prediction can be made about the peptide bitterness. ^prediction

SMILES

N[C@@]([H])(CC(C)C)C(=O)N[C@@]([H])(CC(C)C)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(CC1=CN=C-N1)C(=O)N[C@@]([H])(CC1=CN=C-N1)C(=O)N[C@@]([H])(C)C(=O)N[C@@]([H])(CC(=O)O)C(=O)N[C@@]([H])(C)C(=O)N[C@@]([H])(CC(=O)O)C(=O)N[C@@]([H])(Cc1ccc(O)cc1)C(=O)O

Preparation method

Mode of preparation	Enzymatic hydrolysis
Enzyme(s)/starter culture	Peptide obtained by hydrolysis of a soybean β-conglycinin (7S protein) by use of protease S.

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

N.D

Database cross-references

[D1]

[D2]

[D3]

[D4]

Reference(s)

Primary literature	Chen, H.-M., Muramoto, K., Yamauchi, F. Structural Analysis of Antioxidative Peptides from Soybean .beta.-Conglycinin. Journal of Agricultural and Food Chemistry. 1995, 43, 574-8. DOI: 10.1021/jf00051a004
Other literature(s)	[1] Chen H M, Muramoto K, Yamauchi F, et al. Antioxidant Activity of Designed Peptides Based on the Antioxidative Peptide Isolated from Digests of a Soybean Protein[J]. Journal of Agricultural & Food Chemistry, 1996, 44(9):2619-2623. [2] Huaming Chen †, Koji Muramoto , †, Fumio Yamauchi †, et al. Antioxidative Properties of Histidine-Containing Peptides Designed from Peptide Fragments Found in the Digests of a Soybean Protein.[J]. Journal of Agricultural & Food Chemistry, 1998, 46(1):49.
PubDate	1995