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 - DFBPANCA0015(Anticancer peptide)

DFBP ID	DFBPANCA0015
Peptide sequence	KLPPLLLAKLLMSGKLLAEPCTGR
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

Lys-Leu-Pro-Pro-Leu-Leu-Leu-Ala-Lys-Leu-Leu-Met-Ser-Gly-Lys-Leu-Leu-Ala-Glu-Pro-Cys-Thr-Gly-Arg

Single-letter amino acid

KLPPLLLAKLLMSGKLLAEPCTGR

Peptide length

Peptide mass

Experimental mass	Theoretical mass
2562.405 Da	2563.20 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

10.32 ^c

IC₅₀

N.D

pIC₅₀

N.D

GRAVY

0.4833^c

Hydrophilic residue ratio

66.67%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Animal, Marine, Fish
Organism/Source	Tuna
Precursor protein	Protein hydrolysates from tuna cooking juice
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

Exhibited antiproliferative activity and induced cell cycle arrest in S phase. The tuna cooking juice hydrolysates (PA) showed antiproliferative activities up to 25% against MCF-7 cells, and the > 2.5 kDa ultrafiltration fraction (PAH_2.5) possessed the highest antiproliferative activity with an IC₅₀ value of 1.39 mg/ mL. PAH_2.5 induced cell cycle arrest in S phase through the increases of p21 and p27, and decrease of cyclin A expression. Further, PAH_2.5 also induced apoptosis of MCF-7 cells by downregulation of the expression of Bcl-2, PARP and caspase 9, and upregulation of the expression of p53, Bax and cleaved caspase 3. The peptide was identified in PAH_2.5 as KLPPLLLAKLLMSGKLLAEPCTGR.

Specific target protein(s)

N.D

Taste properties & Structure

Bitterness

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

SMILES

N[C@@]([H])(CCCCN)C(=O)N[C@@]([H])(CC(C)C)C(=O)N1[C@@]([H])(CCC1)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(CC(C)C)C(=O)N[C@@]([H])(CC(C)C)C(=O)N[C@@]([H])(CC(C)C)C(=O)N[C@@]([H])(C)C(=O)N[C@@]([H])(CCCCN)C(=O)N[C@@]([H])(CC(C)C)C(=O)N[C@@]([H])(CC(C)C)C(=O)N[C@@]([H])(CCSC)C(=O)N[C@@]([H])(CO)C(=O)NCC(=O)N[C@@]([H])(CCCCN)C(=O)N[C@@]([H])(CC(C)C)C(=O)N[C@@]([H])(CC(C)C)C(=O)N[C@@]([H])(C)C(=O)N[C@@]([H])(CCC(=O)O)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(CS)C(=O)N[C@@]([H])([C@]([H])(O)C)C(=O)NCC(=O)N[C@@]([H])(CCCNC(=N)N)C(=O)O

Preparation method

Mode of preparation	Enzymatic hydrolysis
Enzyme(s)/starter culture	Tuna cooking juice was hydrolyzed by protease XXIII.

Stability & Cytotoxicity

Peptide stability

Literature report:	N.D
EHP-Tool:	Enzymatic Hydrolysis Prediction Tool (EHP-Tool)

Peptide cytotoxicity

Literature report:	This study has clearly demonstrated that tuna cooking juice has the potential to be a valid protein source of bioactive peptides with the antiproliferative effect on MCF-7 cells and without affecting normal breast epithelial cells.
Prediction:	ToxinPred

Additional information

Tuna cooking juice may be a good protein source of antiproliferative peptides against MCF-7.

Database cross-references

[D1]

[D2]

[D3]

[D4]

Reference(s)

Primary literature	Hung, C.-C., Yang, Y.-H., Kuo, P.-F., Hsu, K.-C. Protein hydrolysates from tuna cooking juice inhibit cell growth and induce apoptosis of human breast cancer cell line MCF-7. Journal of Functional Foods. 2014, 11, 563-70. DOI: 10.1016/j.jff.2014.08.015
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] Huang Y B, Wang X F, Wang H Y, et al. Studies on mechanism of action of anticancer peptides by modulation of hydrophobicity within a defined structural framework[J]. Molecular Cancer Therapeutics, 2011, 10(3):416.
PubDate	2014