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 - DFBPANOX0502(Antioxidative peptide)

DFBP ID	DFBPANOX0502
Peptide sequence	GVPLT
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

Gly-Val-Pro-Leu-Thr

Single-letter amino acid

GVPLT

Peptide length

Peptide mass

Experimental mass	Theoretical mass
485.59 Da	485.58 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

5.97 ^c

IC₅₀

N.D

pIC₅₀

N.D

GRAVY

1.0600^c

Hydrophilic residue ratio

80%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Animal
Organism/Source	Bluefin leatherjacket (Navodon septentrionalis) heads
Precursor protein	Bluefin leatherjacket heads
Residue position	N.D
Precursor protein(s) search	Source.1: DFBPPR0934 ---- Plant proteins ---- LRR receptor-like serine/threonine-protein kinase FLS2 Source.2: DFBPPR2033 ---- Plant proteins ---- Laccase-2 Source.3: DFBPPR2148 ---- Plant proteins ---- Auxin-responsive protein SAUR36 Source.4: DFBPPR2704 ---- Plant proteins ---- DEAD-box ATP-dependent RNA helicase 18 Source.5: DFBPPR2813 ---- Plant proteins ---- Ferrochelatase-1, chloroplastic Source.6: DFBPPR3811 ---- Plant proteins ---- Cytochrome c-type biogenesis CcmH-like mitochondrial protein Source.7: DFBPPR4846 ---- Plant proteins ---- Uncharacterized protein Os04g0629400 Source.8: DFBPPR5405 ---- Plant proteins ---- Terpene synthase 2, chloroplastic Source.9: DFBPPR5682 ---- Plant proteins ---- Probable terpene synthase 3, chloroplastic Source.10: DFBPPR7145 ---- Plant proteins ---- Ferrochelatase-2, chloroplastic Source.11: DFBPPR16027 ---- Animal proteins ---- Rho GTPase-activating protein 35 Source.12: DFBPPR17739 ---- Animal proteins ---- Molybdenum cofactor biosynthesis protein 1 Source.13: DFBPPR19476 ---- Animal proteins ---- Rho GTPase-activating protein 7 Source.14: DFBPPR21707 ---- Animal proteins ---- Mitochondrial import inner membrane translocase subunit Tim23 Source.15: DFBPPR8794 ---- Animal proteins ---- NPC intracellular cholesterol transporter 1 Source.16: DFBPPR9182 ---- Animal proteins ---- Short-chain specific acyl-CoA dehydrogenase, mitochondrial Source.17: DFBPPR15763 ---- Microorganism protein ---- ATPase expression protein 3
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) Peptdie GVPLT showed effective free radical scavenging activity, as shown in Table 1.
(2) The antioxidant activity of GVPLT was due to it small molecular size and the hydrophobic and/or aromatic amino acid residues in its sequence.

Table 1. EC₅₀ values of GVPLT on DPPH•, HO•, O₂^-•, and ABTS•. All data are presented as the mean ± SD of triplicate results.
Peptide	EC₅₀ (mg/ml)
Peptide	DPPH•	HO•	O₂^-•	ABTS•
GVPLT	4.541	4.149	2.881	3.124

Specific target protein(s)

N.D

Taste properties & Structure

Bitterness

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

SMILES

NCC(=O)N[C@@]([H])(C(C)C)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(CC(C)C)C(=O)N[C@@]([H])([C@]([H])(O)C)C(=O)O

Preparation method

Mode of preparation	Enzymatic hydrolysis
Enzyme(s)/starter culture	Head protein, a by-product of bluefin leatherjacket (Navodon septentrionalis) processing, was hydrolyzed by using papain.

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

This research suggests that isolated peptides are excellent antioxidants and could be effectively applied as food ingredients, food additives and pharmaceuticals.

Database cross-references

[D1]

[D2]

[D3]

[D4]

Reference(s)

Primary literature	Chi, C.-F., Wang, B., Wang, Y.-M., Zhang, B., Deng, S.-G. Isolation and characterization of three antioxidant peptides from protein hydrolysate of bluefin leatherjacket (Navodon septentrionalis) heads. Journal of Functional Foods. 2015, 12, 1-10. DOI: 10.1016/j.jff.2014.10.027
Other literature(s)	[1] Zou, T.B., et al., The Structure-Activity Relationship of the Antioxidant Peptides from Natural Proteins. Molecules, 2016. 21(1): p. 72.
PubDate	2015