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 - DFBPANCA0008(Anticancer peptide)

DFBP ID	DFBPANCA0008
Peptide sequence	EQRPR
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

Glu-Gln-Arg-Pro-Arg

Single-letter amino acid

EQRPR

Peptide length

Peptide mass

Experimental mass	Theoretical mass
685.37 Da	684.75 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

10.88 ^c

IC₅₀

N.D

pIC₅₀

N.D

GRAVY

-3.5200^c

Hydrophilic residue ratio

20%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Plant
Organism/Source	Rice
Precursor protein	Rice bran protein
Residue position	N.D
Precursor protein(s) search	Source.1: DFBPPR1447 ---- Plant proteins ---- Two-component response regulator-like PRR37 Source.2: DFBPPR2672 ---- Plant proteins ---- 63 kDa globulin-like protein Source.3: DFBPPR3466 ---- Plant proteins ---- Two-component response regulator-like PRR73 Source.4: DFBPPR4130 ---- Plant proteins ---- Two-component response regulator-like PRR95 Source.5: DFBPPR4633 ---- Plant proteins ---- B3 domain-containing protein Os07g0183700 Source.6: DFBPPR17961 ---- Animal proteins ---- Cyclin-dependent kinase 12 Source.7: DFBPPR21749 ---- Animal proteins ---- Protein CUSTOS Source.8: DFBPPR14303 ---- Marine protein ---- Phycobilisome rod-core linker polypeptide cpcG
Link-research Inductive analysis	Link 1: DFBPANCA0086----Rice----Rice bran

Biological/Functional activity & target protein

Anticancer activity	The peptide EQRPR possess cancer growth inhibitory properties on colon, breast, lung and liver cancer cells. This peptide could serve as a nutraceutical agent against cancer. The pure peptide at 600–700 μg/mL dose caused 84% inhibition to colon cancer cells (Caco-2, HCT-116) growth, 80% to breast cancer cells (MCF-7, MDA-MB-231) growth and 84% to liver cancer cells (HepG-2) growth.
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])(CCC(=O)O)C(=O)N[C@@]([H])(CCC(=O)N)C(=O)N[C@@]([H])(CCCNC(=N)N)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(CCCNC(=N)N)C(=O)O

Preparation method

Mode of preparation	Enzymatic hydrolysis
Enzyme(s)/starter culture	Ground and sieved Heat stabilized De-fatted rice bran was treated with alcalase under optimized conditions to generate peptide hydrolysates, which in turn was passed through simulated gastrointestinal juices and fractionated using ultrafiltration fractionation columns to generate definite molecular sized fractions.

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	Kannan A, Hettiarachchy NS, Lay JO, Liyanage R. Human cancer cell proliferation inhibition by a pentapeptide isolated and characterized from rice bran. Peptides. 2010 Sep;31(9):1629-34. PMID: 20594954 DOI: 10.1016/j.peptides.2010.05.018
Other literature(s)	[1] Kannan A, Hettiarachchy N, Johnson M G, et al. Human colon and liver cancer cell proliferation inhibition by peptide hydrolysates derived from heat-stabilized defatted rice bran.[J]. Agric Food Chem, 2008, 56:11643-11647. [2] Chalamaiah M, Yu W, Wu J. Immunomodulatory and anticancer protein hydrolysates (peptides) from food proteins: A review.[J]. Food Chemistry, 2018, 245:205-222. [3] Ilhan-Ayisigi E, Budak G, Celiktas M S, et al. Anticancer activities of bioactive peptides derived from rice husk both in free and encapsulated form in chitosan.[J]. Journal of Industrial and Engineering Chemistry, 2021, 103:381-391.
PubDate	2010