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 - DFBPANCA0009(Anticancer peptide)

DFBP ID	DFBPANCA0009
Peptide sequence	VECYGPNRPQF
Type	Native peptide
Peptide/Function name	Anticancer peptide

Function-activity relationship

Main bioactivity	Anticancer activity
Otheir bioactivity	ACE-inhibitory activity ^[D1], Antioxidative 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, Marine
Organism/Source	Algae (Chlorella vulgaris)
Precursor protein	Algae protein waste
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

Anticancer activity

The peptide fraction had strong dose-dependent antiproliferation and induced a post-G1 cell cycle arrest in AGS cells; however, no cytotoxicity was observed in WI-38 lung fibroblasts cells in vitro. The peptide fraction also revealed much better antioxidant activity toward peroxyl radicals and LDL than those of Trolox. Among these peptides, the hendecapeptide VECYGPNRPQF has a potent antiproliferative (IC₅₀ value of 256.4 ± 1.2 μM against human gastric cancer cell lines AGS), antioxidant^[D2], and NO-production-inhibiting activity.

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 (The yield was approximately 0.94%).

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

Algae protein waste is a by-product during production of algae essence from Chlorella vulgaris and the literature suggested that inexpensive algae protein waste could be a new alternative to produce anticancer peptides.

Database cross-references

DFBP

[D1]	DFBPACEI0123
[D2]	DFBPANOX0166
[D3]	DFBPMUFU0052

BIOPEP-UWM

[D4]

8137, 8138, 8997

APD

[D5]

BioPepDB

[D6]

MBPDB

[D7]

Reference(s)

Primary literature	Sheih IC, Fang TJ, Wu TK, Lin PH. Anticancer and antioxidant activities of the peptide fraction from algae protein waste. J Agric Food Chem. 2010 Jan 27;58(2):1202-7. PMID: 19916544 DOI: 10.1021/jf903089m
Other literature(s)	[1] Chalamaiah M, Yu W, Wu J. Immunomodulatory and anticancer protein hydrolysates (peptides) from food proteins: A review.[J]. Food Chemistry, 2018, 245:205-222.
PubDate	2010