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 - DFBPANCA0002(Anticancer peptide)

DFBP ID	DFBPANCA0002
Peptide sequence	WMLPSYSPY
Type	Native peptide
Peptide/Function name	Anticancer peptide

Function-activity relationship

Main bioactivity	Anticancer activity
Otheir bioactivity	N.D

Calculated physicochemical properties

Three-letter amino acid

Trp-Met-Leu-Pro-Ser-Tyr-Ser-Pro-Tyr

Single-letter amino acid

WMLPSYSPY

Peptide length

Peptide mass

Experimental mass	Theoretical mass
1157 Da	1143.31 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

5.87 ^c

IC₅₀

N.D

pIC₅₀

N.D

GRAVY

-0.2889^c

Hydrophilic residue ratio

55.56%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Plant
Organism/Source	Soybean
Precursor protein	Defatted soy protein
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

Anticancer activity of each fraction was assayed by measuring in vitro cytotoxicity on P388D1, a mouse monocyte macrophage cell line. IC₅₀ value of a peptide fraction from Sephadex G-25 chromatography was 0.16 mg/ml. This peptide fraction at 1 mg/ml significantly affected cell cycle progression by arresting P388D1 at G2/M phases. Cell growth inhibition and significantly affected cell cycle progression by arresting P388D1 at G2/M phases.

Fig. 1. In vitro cytotoxicity of Sephadex G-25 fractions on P388D1, a mouse monocyte macrophage cell line. The cytotoxic effect was determined by the viability of the cells treated with the hydrolyzate of soybean proteins. The viability of the cells was
measured by ³H-thymidine uptake after 72 h incubation. The percent cytotoxicity was calculated using the following formula: % Cytotoxicity = (1 — cpm in sample/cpm in control) × 100. Each treatment group included at least three samples.

Fig. 2. Effects of fractionated soy peptides on the cell cycle progression of P388D1. P388D1 cells were incubated 12 h treated with To4 fraction at 1 mg/ml [A]. Untreated cells were used for control [B]. After incubation, cells were washed and stained with propiodium iodide, DNA staining/lysis solution, containing EDTA and detergents. The suspension cells were analyzed by FACS. DNA content of each phase was analyzed by Modifit LT software.

Specific target protein(s)

N.D

Taste properties & Structure

Bitterness

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

SMILES

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

Structure

Embedded Mol* Viewer

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Docking

Embedded Mol* Viewer

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Preparation method

Mode of preparation	Enzymatic hydrolysis
Enzyme(s)/starter culture	Defatted soy protein was hydrolyzed with thermoase and hydrophobic peptides were extracted with ethanol.

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

The peptide was a hydrophobic peptide.
The sequence in the literature was X-MLPSYSPY, but we infer that the X may be was Trp based on relative molecular mass.
These results suggest that peptides could be utilized as new materials to develop functional foods with cancer reducing activity.

Database cross-references

[D1]

[D2]

[D3]

[D4]

Reference(s)

Primary literature	Kim SE, Kim HH, Kim JY, Kang YI, Woo HJ, Lee HJ. Anticancer activity of hydrophobic peptides from soy proteins. Biofactors. 2000;12(1-4):151-5. PMID: 11216478 DOI: 10.1002/biof.5520120124
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. [2] Udenigwe C C , Hannah W , Gong M , et al. Preclinical Evidence on the Anticancer Properties of Food Peptides[J]. Protein Pept Lett, 2017, 24(2):-.
PubDate	2000