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List of peptide properties
DFBP ID - DFBPANOX0302(Antioxidative peptide)
DFBP ID DFBPANOX0302
Peptide sequence PAGY
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 Pro-Ala-Gly-Tyr
Single-letter amino acid PAGY
Peptide length 4
Peptide mass
Experimental mass Theoretical mass
457 Da 406.43 Da c
Net charge 0.00 c
Isoelectric point (pI) 5.92 c
IC50 N.D
pIC50 N.D
GRAVY -0.3750 c
Hydrophilic residue ratio 75% c
Peptide calculator
To calculate the physicochemical properties of bioactive peptide.
Peptide source & Food-borne protein(s) search
Classification Animal, Fish, Marine
Organism/Source Tuna
Precursor protein Tuna cooking juice
Residue position N.D
Precursor protein(s) search
Source.1: DFBPPR0829 ---- Plant proteins ---- Homeobox-leucine zipper protein ROC5
Source.2: DFBPPR0830 ---- Plant proteins ---- Homeobox-leucine zipper protein ROC6
Source.3: DFBPPR0964 ---- Plant proteins ---- Thioredoxin reductase NTRC
Source.4: DFBPPR1424 ---- Plant proteins ---- Germin-like protein 8-14
Source.5: DFBPPR3171 ---- Plant proteins ---- Putrescine hydroxycinnamoyltransferase
Source.6: DFBPPR3390 ---- Plant proteins ---- Probable nucleoredoxin 1-2
Source.7: DFBPPR3703 ---- Plant proteins ---- Zinc-finger homeodomain protein 1
Source.8: DFBPPR3704 ---- Plant proteins ---- Zinc-finger homeodomain protein 2
Source.9: DFBPPR3953 ---- Plant proteins ---- DEAD-box ATP-dependent RNA helicase 16
Source.10: DFBPPR4762 ---- Plant proteins ---- Zinc finger CCCH domain-containing protein 35
Source.11: DFBPPR4990 ---- Plant proteins ---- Beta-conglycinin alpha' subunit
Source.12: DFBPPR5025 ---- Plant proteins ---- Beta-conglycinin alpha subunit 1
Source.13: DFBPPR5036 ---- Plant proteins ---- Beta-conglycinin alpha subunit 2
Source.14: DFBPPR5570 ---- Plant proteins ---- ATP synthase subunit beta, mitochondrial
Source.15: DFBPPR6396 ---- Plant proteins ---- Hydroxyproline O-arabinosyltransferase NOD3
Source.16: DFBPPR7469 ---- Plant proteins ---- Germin-like protein 1
Source.17: DFBPPR16131 ---- Animal proteins ---- Pyruvate kinase PKLR
Source.18: DFBPPR16224 ---- Animal proteins ---- Uromodulin
Source.19: DFBPPR16646 ---- Animal proteins ---- AT-rich interactive domain-containing protein 5B
Source.20: DFBPPR17228 ---- Animal proteins ---- Lanosterol synthase
Source.21: DFBPPR17576 ---- Animal proteins ---- Fibrillin-1
Source.22: DFBPPR17626 ---- Animal proteins ---- Elastin
Source.23: DFBPPR18072 ---- Animal proteins ---- Postacrosomal sheath WW domain-binding protein
Source.24: DFBPPR18402 ---- Animal proteins ---- Uromodulin
Source.25: DFBPPR18511 ---- Animal proteins ---- Complement C1s subcomponent
Source.26: DFBPPR18737 ---- Animal proteins ---- Centrosomal protein of 120 kDa
Source.27: DFBPPR18794 ---- Animal proteins ---- LIM domain-containing protein ajuba
Source.28: DFBPPR18908 ---- Animal proteins ---- Proteasome subunit alpha type-6
Source.29: DFBPPR19600 ---- Animal proteins ---- Macrophage-expressed gene 1 protein
Source.30: DFBPPR20060 ---- Animal proteins ---- Fibulin-5
Source.31: DFBPPR20142 ---- Animal proteins ---- Kinesin-like protein KIF3C
Source.32: DFBPPR20486 ---- Animal proteins ---- Ethanolamine-phosphate phospho-lyase
Source.33: DFBPPR20674 ---- Animal proteins ---- Stromal membrane-associated protein 2
Source.34: DFBPPR20914 ---- Animal proteins ---- AT-rich interactive domain-containing protein 5B
Source.35: DFBPPR21101 ---- Animal proteins ---- Bromodomain-containing protein 2
Source.36: DFBPPR21111 ---- Animal proteins ---- Zinc finger protein-like 1
Source.37: DFBPPR21125 ---- Animal proteins ---- Male-enhanced antigen 1
Source.38: DFBPPR21261 ---- Animal proteins ---- tRNA selenocysteine 1-associated protein 1
Source.39: DFBPPR21492 ---- Animal proteins ---- Homeobox protein DBX1
Source.40: DFBPPR22053 ---- Animal proteins ---- Protein FAM118B
Source.41: DFBPPR8591 ---- Animal proteins ---- Glutathione hydrolase 1 proenzyme
Source.42: DFBPPR8923 ---- Animal proteins ---- Cubilin
Source.43: DFBPPR9102 ---- Animal proteins ---- Nuclear factor of activated T-cells, cytoplasmic 1
Source.44: DFBPPR9865 ---- Animal proteins ---- Male-enhanced antigen 1
Source.45: DFBPPR10218 ---- Animal proteins ---- Occludin
Source.46: DFBPPR10501 ---- Animal proteins ---- Very low-density lipoprotein receptor
Source.47: DFBPPR10520 ---- Animal proteins ---- Collagen alpha-2(IX) chain
Source.48: DFBPPR10668 ---- Animal proteins ---- E3 UFM1-protein ligase 1
Source.49: DFBPPR10735 ---- Animal proteins ---- Semaphorin-3E
Source.50: DFBPPR10953 ---- Animal proteins ---- DNA repair and recombination protein RAD54-like
Source.51: DFBPPR11314 ---- Animal proteins ---- Multivesicular body subunit 12A
Source.52: DFBPPR11771 ---- Animal proteins ---- Homeobox protein goosecoid
Source.53: DFBPPR11963 ---- Animal proteins ---- Stromal membrane-associated protein 2
Source.54: DFBPPR11996 ---- Animal proteins ---- Homeobox protein Hox-A6
Source.55: DFBPPR12310 ---- Animal proteins ---- Voltage-dependent L-type calcium channel subunit alpha-1C
Source.56: DFBPPR12422 ---- Animal proteins ---- Voltage-dependent R-type calcium channel subunit alpha-1E
Source.57: DFBPPR12453 ---- Animal proteins ---- Lactase-phlorizin hydrolase
Source.58: DFBPPR12835 ---- Animal proteins ---- Chloride channel protein ClC-Ka
Source.59: DFBPPR15876 ---- Microorganism protein ---- Probable DNA-directed RNA polymerase
Source.60: DFBPPR0003 ---- Plant protein ---- Conglutin beta 2
Source.61: DFBPPR0009 ---- Plant protein ---- Conglutin beta 1
Source.62: DFBPPR7960 ---- Plant protein ---- Vicilin
Link-research
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 showed potent 1,1-diphenyl-2-picrylhydrzyl (DPPH) scavenging activity with a scavenging effect of 75% at concentration of 87 μg/mL.

Specific target protein(s) N.D
Taste properties & Structure
Bitterness
Literature report N.D
Bitter prediction tools Bitter taste prediction
SMILES N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(C)C(=O)NCC(=O)N[C@@]([H])(Cc1ccc(O)cc1)C(=O)O
Preparation method
Mode of preparation Enzymatic hydrolysis
Enzyme(s)/starter culture

Protease XXIII, from Aspergillus oryzae, was used to hydrolyze tuna cooking juice at 37 ℃ for up to 6 h.

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
Additional information

Hydrolyzates from tuna cooking juice, and the fractions derived from them, can be incorporated into lipid-containing foods as chain-breaking antioxidants to minimize free radical-mediated lipid peroxidation. These hydrolyzates can also be used as alternatives to conventional drugs for treating human diseases associated with free radical-mediated tissue damage.

Database cross-references
BIOPEP-UWM [D1] 8087
APD [D2] -
BioPepDB [D3] -
MBPDB [D4] -
Reference(s)
Primary literature Jao, C.-L., Ko, W.-C. 1,1-Diphenyl-2-picrylhydrazyl (DPPH) radical scavenging by protein hydrolyzates from tuna cooking juice. Fisheries Science. 2002, 68, 430-5.
Other literature(s) N.D
PubDate 2002
Copyright © 2020. Record / license number: Chongqing ICP No. 2000214