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 - DFBPANCA0329(Anticancer peptide)

DFBP ID	DFBPANCA0329
Peptide sequence	VFDGEL
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

Val-Phe-Asp-Gly-Glu-Leu

Single-letter amino acid

VFDGEL

Peptide length

Peptide mass

Experimental mass	Theoretical mass
678.36 Da	678.73 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

3.04 ^c

IC₅₀

N.D

pIC₅₀

N.D

GRAVY

0.5667^c

Hydrophilic residue ratio

66.67%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Plant
Organism/Source	Soybean
Precursor protein	Glycinin G1, G2, G3 subunit
Residue position	N.D
Precursor protein(s) search	Source.1: DFBPPR2151 ---- Plant proteins ---- Glutelin type-A 3 Source.2: DFBPPR4965 ---- Plant proteins ---- Glycinin G1 Source.3: DFBPPR4966 ---- Plant proteins ---- Glycinin G5 Source.4: DFBPPR4973 ---- Plant proteins ---- Glycinin G2 Source.5: DFBPPR4992 ---- Plant proteins ---- Glycinin G3 Source.6: DFBPPR4995 ---- Plant proteins ---- Glycinin G4 Source.7: DFBPPR6380 ---- Plant proteins ---- Legumin A Source.8: DFBPPR6425 ---- Plant proteins ---- Legumin A2
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

Topoisomerases are targets of several anticancer agents because their inhibition impedes the processes of cell proliferation and differentiation in carcinogenesis. The synthetic peptide VFDGEL was used to confirm the inhibitory activity on topoisomerase II, and its IC₅₀ value was 7.9 mM.
The molecular interactions of three peptides (FEITPEKNPQ, IETWNPNNKP, VFDGEL) evaluated by molecular docking revealed interaction energies with the topoisomerase II C-terminal domain (CTD) (-186 to -398 kcal/mol) that were smaller than for the ATPase domain (-169 to -357 kcal/mol) and that correlated well with our experimental IC₅₀ values (R² = 0.99). In conclusion, three peptides released from in vitro gastrointestinal enzyme digestion of soy proteins inhibited human topoisomerase II activity through binding to the active site of the CTD domain.
A homology model generated from the yeast topoisomerase II structure (PDB ID: 1BGW) template had been successfully used in structure-based virtual screening of human topoisomerase II inhibitors. Yeast topoisomerase II ATPase structure was downloaded from the Protein Data Bank (PDB ID:1QZR).

Table 1. Human DNA Topoisomerase II Inhibitory Activities and Interaction Energy of Molecular Docking of Three Peptides against Human Topoisomerase II CTD Domain and ATPase Domain ^a
topoisomerase II inhibitor	interaction energy (kcal/mol)		IC₅₀ (mM) of synthetic peptides
topoisomerase II inhibitor	CTD domain	ATPase domain	IC₅₀ (mM) of synthetic peptides
FEITPEKNPQ	-398.1	-254.9	2.4
IETWNPNNKP	-355.0	-356.8	4.0
VFDGEL	-186.0	-168.7	7.9
^a The interaction energy was calculated using the potential energy function in MOE. The lower the energy, the stronger the binding is. The IC₅₀ values of peptides were determined by cytotoxicity assay with custom synthetic peptides.

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])(Cc1ccccc1)C(=O)N[C@@]([H])(CC(=O)O)C(=O)NCC(=O)N[C@@]([H])(CCC(=O)O)C(=O)N[C@@]([H])(CC(C)C)C(=O)O

Preparation method

Mode of preparation	Enzymatic hydrolysis
Enzyme(s)/starter culture	Soy protein isolates were subjected to simulated gastrointestinal digestion with pepsin and pancreatin, and the human topoisomerase II inhibitory peptides were co-immunoprecipitated and identified on a CapLC- Micromass Q-TOF Ultima API system.

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

N.D

Database cross-references

[D1]

[D2]

[D3]

[D4]

Reference(s)

Primary literature	Wang W, Rupasinghe SG, Schuler MA, Gonzalez de Mejia E. Identification and characterization of topoisomerase II inhibitory peptides from soy protein hydrolysates. J Agric Food Chem. 2008 Aug 13;56(15):6267-77. PMID: 18593177 DOI: 10.1021/jf8005195
Other literature(s)	[1] 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	2008