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 - DFBPANCA0095(Anticancer peptide)

DFBP ID	DFBPANCA0095
Peptide sequence	KENPVLSLVNGMF
Type	Native peptide
Peptide/Function name	Anticancer peptide

Function-activity relationship

Main bioactivity	Anticancer activity
Otheir bioactivity	Cytotoxic activity ^[D1], Multifunctional activity ^[D2]

Calculated physicochemical properties

Three-letter amino acid

Lys-Glu-Asn-Pro-Val-Leu-Ser-Leu-Val-Asn-Gly-Met-Phe

Single-letter amino acid

KENPVLSLVNGMF

Peptide length

Peptide mass

Experimental mass	Theoretical mass
1447.70 Da	1447.71 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

6.92 ^c

IC₅₀

N.D

pIC₅₀

N.D

GRAVY

0.2692^c

Hydrophilic residue ratio

61.54%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Marine
Organism/Source	Marine sponge Xestospongia testudinaria
Precursor protein	The protein hydrolysates of X. testudinaria
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 synthetic peptide KENPVLSLVNGMF showed cytotoxicity toward HeLa cells in a dose-dependent manner and the peptide (EC₅₀ 0.67 mM) was 3.8-fold more cytotoxic compared with anticancer drug 5-fluorouracil (EC₅₀ 2.56 mM). The peptide was non-cytotoxic against non-cancerous Hek293 cells.
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])(CCCCN)C(=O)N[C@@]([H])(CCC(=O)O)C(=O)N[C@@]([H])(CC(=O)N)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(C(C)C)C(=O)N[C@@]([H])(CC(C)C)C(=O)N[C@@]([H])(CO)C(=O)N[C@@]([H])(CC(C)C)C(=O)N[C@@]([H])(C(C)C)C(=O)N[C@@]([H])(CC(=O)N)C(=O)NCC(=O)N[C@@]([H])(CCSC)C(=O)N[C@@]([H])(Cc1ccccc1)C(=O)O

Preparation method

Mode of preparation	Enzymatic hydrolysis
Enzyme(s)/starter culture	Comparison among trypsin, chymotrypsin, papain and alcalase hydrolysates of X. testudinaria revealed papain hydrolysate to be the most active.

Stability & Cytotoxicity

Peptide stability

Literature report:	The half-life of the peptide was 3.2 ± 0.5 h in human serum in vitro, as revealed by RP-HPLC analyses.
EHP-Tool:	Enzymatic Hydrolysis Prediction Tool (EHP-Tool)

Peptide cytotoxicity

Literature report:	The peptide KENPVLSLVNGMF showed only marginal 5% cytotoxicity to Hek293, a non-cancerous, human embryonic kidney cell line, but 44% cytotoxicity in HeLa cells when tested at 0.67 mM.
Prediction:	ToxinPred

Additional information

The peptide KENPVLSLVNGMF identified from X. testudinaria papain hydrolysate has potential applications as peptide lead in future development of potent and specific anticancer drugs.

Database cross-references

DFBP

[D1]	DFBPCYPE0006
[D2]	DFBPMUFU0718

[D3]

[D4]

[D5]

[D6]

Reference(s)

Primary literature	Quah, Y., Mohd Ismail, N.I., Ooi, J.L.S., Affendi, Y.A., Abd Manan, F., Wong, F.-C., et al. Identification of Novel Cytotoxic Peptide KENPVLSLVNGMF from Marine Sponge Xestospongia testudinaria, with Characterization of Stability in Human Serum. International Journal of Peptide Research and Therapeutics. 2017, 24, 189-99. DOI: 10.1007/s10989-017-9604-6
Other literature(s)	N.D
PubDate	2017