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 - DFBPANOX0582(Antioxidative peptide)

DFBP ID	DFBPANOX0582
Peptide sequence	APIRMWYMYRKLTDMEPKPVA
Type	Native peptide
Peptide/Function name	Antioxidative peptide

Function-activity relationship

Main bioactivity	Antioxidative activity
Otheir bioactivity	N.D

Calculated physicochemical properties

Three-letter amino acid

Ala-Pro-Ile-Arg-Met-Trp-Tyr-Met-Tyr-Arg-Lys-Leu-Thr-Asp-Met-Glu-Pro-Lys-Pro-Val-Ala

Single-letter amino acid

APIRMWYMYRKLTDMEPKPVA

Peptide length

Peptide mass

Experimental mass	Theoretical mass
N.D	2597.13 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

9.95 ^c

IC₅₀

N.D

pIC₅₀

N.D

GRAVY

-0.5238^c

Hydrophilic residue ratio

57.14%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Animal
Organism/Source	N.D
Precursor protein	Frog skin
Residue position	N.D
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

Antioxidative activity	The peptide APIRMWYMYRKLTDMEPKPVA possessed strong DPPH and ABTS^.+ scavenging activities, and effectively inhibited lipid peroxidation in linoleic acid emulsion system during a 7-day test.
Specific target protein(s)	N.D

Taste properties & Structure

Bitterness

Literature report	N.D
Bitter prediction tools	Bitter taste ^prediction

SMILES

N[C@@]([H])(C)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])([C@]([H])(CC)C)C(=O)N[C@@]([H])(CCCNC(=N)N)C(=O)N[C@@]([H])(CCSC)C(=O)N[C@@]([H])(CC(=CN2)C1=C2C=CC=C1)C(=O)N[C@@]([H])(Cc1ccc(O)cc1)C(=O)N[C@@]([H])(CCSC)C(=O)N[C@@]([H])(Cc1ccc(O)cc1)C(=O)N[C@@]([H])(CCCNC(=N)N)C(=O)N[C@@]([H])(CCCCN)C(=O)N[C@@]([H])(CC(C)C)C(=O)N[C@@]([H])([C@]([H])(O)C)C(=O)N[C@@]([H])(CC(=O)O)C(=O)N[C@@]([H])(CCSC)C(=O)N[C@@]([H])(CCC(=O)O)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(CCCCN)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(C(C)C)C(=O)N[C@@]([H])(C)C(=O)O

Preparation method

Mode of preparation	Extract
Enzyme(s)/starter culture	The peptide was purified from skin secretions.

Stability & Cytotoxicity

Peptide stability

Literature report:	N.D
EHP-Tool:	Enzymatic Hydrolysis Prediction Tool (EHP-Tool)

Peptide cytotoxicity

Literature report:	No cytotoxic and hemolytic activity against human erythrocytes was observed for the peptide.
Prediction:	ToxinPred

Additional information

N.D

Database cross-references

[D1]

[D2]

[D3]

[D4]

Reference(s)

Primary literature	Yu H, Qiao X, Gao J, Wang C, Cai S, Feng L, Wang H, Wang YP. Identification and Characterization of Novel Antioxidant Peptides Involved in Redox Homeostasis of Frog, Limnonectes fragilis. Protein Pept Lett. 2015;22(9):776-84. PMID: 26122987 DOI: 10.2174/0929866522666150630104815
Other literature(s)	N.D
PubDate	2015