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 - DFBPANCA0010(Anticancer peptide)

DFBP ID	DFBPANCA0010
Peptide sequence	LPHVLTPEAGAT
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

Leu-Pro-His-Val-Leu-Thr-Pro-Glu-Ala-Gly-Ala-Thr

Single-letter amino acid

LPHVLTPEAGAT

Peptide length

Peptide mass

Experimental mass	Theoretical mass
1206 Da	1205.36 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

5.17 ^c

IC₅₀

N.D

pIC₅₀

N.D

GRAVY

0.3083^c

Hydrophilic residue ratio

66.67%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Animal, Marine, Fish
Organism/Source	Tuna dark
Precursor protein	Tuna dark muscle byproduct 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	The peptide LPHVLTPEAGAT possessed antiproliferative activity and it showed the dose-dependent inhibition effect of the human breast cancer (MCF-7) cells with IC₅₀ values of 8.1 μM.
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])(CC(C)C)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(CC1=CN=C-N1)C(=O)N[C@@]([H])(C(C)C)C(=O)N[C@@]([H])(CC(C)C)C(=O)N[C@@]([H])([C@]([H])(O)C)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(CCC(=O)O)C(=O)N[C@@]([H])(C)C(=O)NCC(=O)N[C@@]([H])(C)C(=O)N[C@@]([H])([C@]([H])(O)C)C(=O)O

Structure

Embedded Mol* Viewer

Docking

Embedded Mol* Viewer

Preparation method

Mode of preparation	Enzymatic hydrolysis
Enzyme(s)/starter culture	Tuna dark muscle byproduct was hydrolyzed by two commercial enzymes, papain and protease XXIII.

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

Antiproliferative hydrolysates from tuna dark muscle byproduct may be useful ingredients in food and nutraceutical applications.

Database cross-references

[D1]

[D2]

[D3]

[D4]

Reference(s)

Primary literature	Hsu, K.-C., Li-Chan, E.C.Y., Jao, C.-L. Antiproliferative activity of peptides prepared from enzymatic hydrolysates of tuna dark muscle on human breast cancer cell line MCF-7. Food Chem. 2011, 126, 617-22. DOI: 10.1016/j.foodchem.2010.11.066
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	2011