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 - DFBPANCA0021(Anticancer peptide)

DFBP ID	DFBPANCA0021
Peptide sequence	MTEEY
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

Met-Thr-Glu-Glu-Tyr

Single-letter amino acid

MTEEY

Peptide length

Peptide mass

Experimental mass	Theoretical mass
671.98 Da	671.72 Da ^c

Net charge

-2

Isoelectric point (pI)

2.94

IC₅₀

N.D

pIC₅₀

N.D

GRAVY

-1.4200^c

Hydrophilic residue ratio

20%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Plant
Organism/Source	Common bean (Phaseolus vulgaris)
Precursor protein	N.D
Residue position	N.D
Precursor protein(s) search	Source.1: DFBPPR2159 ---- Plant proteins ---- NAD(P)H-quinone oxidoreductase subunit I, chloroplastic Source.2: DFBPPR5122 ---- Plant proteins ---- NAD(P)H-quinone oxidoreductase subunit I, chloroplastic Source.3: DFBPPR5741 ---- Plant proteins ---- NAD(P)H-quinone oxidoreductase subunit I, chloroplastic Source.4: DFBPPR6733 ---- Plant proteins ---- NAD(P)H-quinone oxidoreductase subunit I, chloroplastic Source.5: DFBPPR7133 ---- Plant proteins ---- NAD(P)H-quinone oxidoreductase subunit I, chloroplastic Source.6: DFBPPR17737 ---- Animal proteins ---- Inactive serine/threonine-protein kinase TEX14 Source.7: DFBPPR7795 ---- Plant protein ---- NAD(P)H-quinone oxidoreductase subunit I, chloroplastic Source.8: DFBPPR8066 ---- Plant protein ---- NAD(P)H-quinone oxidoreductase subunit I, chloroplastic Source.9: DFBPPR8236 ---- Plant protein ---- NAD(P)H-quinone oxidoreductase subunit I, chloroplastic
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

Cell growth inhibition, and modified the expression of cell cycle regulatory proteins p53, p21, cyclin B1, BAD, cytC, c-casp3, Survivin, and BIRC7. The peptide contributed to the antiproliferative effect on human colorectal cancer cells by modifying molecules involved in either cell cycle arrest or apoptosis. Based on the antiproliferative effect, HCT116 cell line was most sensitive to bean Azufrado Higuera (IC₅₀ = 0.53 mg/ml) and RKO to Bayo Madero (IC₅₀ = 0.51 mg/ml) peptide extracts. Both cultivars increased significantly (p < 0.05) the expression of p53 in HCT116 by 76% and 68%, respectively. Azufrado Higuera modified the expression of cell cycle regulation proteins p21 and cyclin B1. Bayo Madero modified the expression of mitochondrial activated apoptotic proteins BAD, cytC, c-casp3, Survivin, BIRC7.

Specific target protein(s)

N.D

Taste properties & Structure

Bitterness

Literature report	N.D
Bitter prediction tools	Non-bitter taste ^prediction

SMILES

N[C@@]([H])(CCSC)C(=O)N[C@@]([H])([C@]([H])(O)C)C(=O)N[C@@]([H])(CCC(=O)O)C(=O)N[C@@]([H])(CCC(=O)O)C(=O)N[C@@]([H])(Cc1ccc(O)cc1)C(=O)O

Structure

Embedded Mol* Viewer

Docking

Embedded Mol* Viewer

Preparation method

Mode of preparation	Enzymatic hydrolysis
Enzyme(s)/starter culture	A sequential enzyme digestion was performed with pepsin and pancreatin at 37 ℃ for 1.5 h for each enzyme.

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 hydrophobicity of peptide was +14.03 Kcal/mol.

Database cross-references

DFBP

[D1]	DFBPACEI1030
[D2]	DFBPANOX0516
[D3]	DFBPMUFU0526

[D4]

[D5]

[D6]

[D7]

Reference(s)

Primary literature	Luna Vital DA, González de Mejía E, Dia VP, Loarca-Piña G. Peptides in common bean fractions inhibit human colorectal cancer cells. Food Chem. 2014 Aug 15;157:347-55. PMID: 24679790 DOI: 10.1016/j.foodchem.2014.02.050
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	2014