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 - DFBPANOX0166(Antioxidative peptide)

DFBP ID	DFBPANOX0166
Peptide sequence	VECYGPNRPQF
Type	Native peptide
Peptide/Function name	Antioxidative peptide

Function-activity relationship

Main bioactivity	Antioxidative activity
Otheir bioactivity	ACE-inhibitory activity ^[D1], Anticancer activity ^[D2], Multifunctional activity ^[D3]

Calculated physicochemical properties

Three-letter amino acid

Val-Glu-Cys-Tyr-Gly-Pro-Asn-Arg-Pro-Gln-Phe

Single-letter amino acid

VECYGPNRPQF

Peptide length

Peptide mass

Experimental mass	Theoretical mass
1309 Da	1309.47 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

6.29 ^c

IC₅₀

N.D

pIC₅₀

N.D

GRAVY

-0.9455^c

Hydrophilic residue ratio

45.45%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Plant
Organism/Source	Microalgae (Chlorella vulgaris)
Precursor protein	Algae protein waste hydrolysates
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 could efficiently quench a variety of free radicals, including hydroxyl radical (IC₅₀ value: 8.3 ± 0.15 uM), superoxide radical (IC₅₀ value: 7.5 ± 0.12 uM), peroxyl radical, DPPH radical (IC₅₀ value: 58.0 ± 1.2 uM) and ABTS radicals (IC₅₀ value: 9.8 ± 0.5 uM), and performed more efficiently than that observed for BHT, Trolox and peptides from marine protein sources in most cases. The antioxidative activity against peroxyl radicals was in the order of purified peptide > ascorbic acid > BHT, indicating that purified peptide was more active than the three reference antioxidants.

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])(C(C)C)C(=O)N[C@@]([H])(CCC(=O)O)C(=O)N[C@@]([H])(CS)C(=O)N[C@@]([H])(Cc1ccc(O)cc1)C(=O)NCC(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(CC(=O)N)C(=O)N[C@@]([H])(CCCNC(=N)N)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(CCC(=O)N)C(=O)N[C@@]([H])(Cc1ccccc1)C(=O)O

Preparation method

Mode of preparation	Enzymatic hydrolysis
Enzyme(s)/starter culture	Peptide obtained by hydrolysis of algae protein waste by use of pepsin pepsin at 50 ℃ for 15 h.

Stability & Cytotoxicity

Peptide stability

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

Peptide cytotoxicity

Literature report:

(1) The purified peptide had the protective capacity increased with increasing peptide concentrations ranging from 10.6 to 84.9 uM in oxidation-incudced DNA damage.
(2) The peptide has gastrointestinal enzyme-resistance and no cytotoxicity observed in human lung fibroblasts cell lines (WI-38) in vitro.
(3) The viability of AGS cells increased by 40% at 0.15 mM dosage of the peptide, compared with that of the cells without peptide pretreatment (data not shown).

Prediction:

ToxinPred

Additional information

Inexpensive algae protein waste could be a new alternative to produce antioxidative peptides.

Database cross-references

DFBP

[D1]	DFBPACEI0123
[D2]	DFBPANCA0009
[D3]	DFBPMUFU0052

BIOPEP-UWM

[D4]

8137, 8138, 8997

APD

[D5]

BioPepDB

[D6]

MBPDB

[D7]

Reference(s)

Primary literature	Sheih IC, Wu TK, Fang TJ. Antioxidant properties of a new antioxidative peptide from algae protein waste hydrolysate in different oxidation systems. Bioresour Technol. 2009 Jul;100(13):3419-25. PMID: 19299123 DOI: 10.1016/j.biortech.2009.02.014
Other literature(s)	[1] Sheih I C, Fang T J, Wu T K, et al. Anticancer and antioxidant activities of the peptide fraction from algae protein waste.[J]. Journal of Agricultural & Food Chemistry, 2010, 58(2):1202-7. [2] Sheih, I. C, Fang, T. J, Wu TungKung. Isolation and characterisation of a novel angiotensin I-converting enzyme (ACE) inhibitory peptide from the algae protein waste.[J]. Food Chemistry, 2009, 115(1):279-284. additional information: Algae protein waste is a by-product during production of algae essence from Chlorella vulgaris.
PubDate	2009