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 - DFBPANCA0003(Anticancer peptide)

DFBP ID	DFBPANCA0003
Peptide sequence	FKCRRWQWRMKKLGAPSITCVR
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

Phe-Lys-Cys-Arg-Arg-Trp-Gln-Trp-Arg-Met-Lys-Lys-Leu-Gly-Ala-Pro-Ser-Ile-Thr-Cys-Val-Arg

Single-letter amino acid

FKCRRWQWRMKKLGAPSITCVR

Peptide length

Peptide mass

Experimental mass	Theoretical mass
2753.88 Da	2751.37 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

12.07 ^c

IC₅₀

N.D

pIC₅₀

N.D

GRAVY

-0.6591^c

Hydrophilic residue ratio

45.45%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Animal
Organism/Source	Bovine milk
Precursor protein	Lactoferrin
Residue position	f(17-38)
Precursor protein(s) search	Source.1: DFBPPR8500 ---- Milk proteins ---- Lactotransferrin
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 1 showed cell proliferation inhibition activity in human leukemic (HL-60) cells due to induction of apoptosis and among the four peptides, peptide 1 was found to exhibit highest activity, as shown in table 1.

Table 1. Amino acid sequence of the cell proliferation inhibitor from pepsin-digested lactoferrin and the concentration of the inhibitor needed to inhibit the cell proliferation by 50%.
Peptide No.	N-terminal sequence	Position in lactoferrin	Molecular mass	IC₅₀
Peptide No.	N-terminal sequence	Position in lactoferrin	Molecular mass	μM	μg/ml
Peptide 1	FKCRRWQWRMKKLGAPSITCVR	17-38	2753.88	2.22	6.1
Peptide 2	APRKNVRWCTISQPEWCIRA ^a	(1-16)-(45-48)	2430.13	11.9	28.9
Peptide 3	APRKNVRWCTISQPECI ^a	(1-15)-(45-46)	2017.92	ND	ND
Peptide 4	APRKNVRWCTISQ	1-13	1558.73	22.1	34.5

^a Peptide 2 and Peptide 3 were linked by disulfide-bridge (The position of the disulfide bond was the amino acids with yellow background).

Specific target protein(s)

N.D

Taste properties & Structure

Bitterness

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

SMILES

N[C@@]([H])(Cc1ccccc1)C(=O)N[C@@]([H])(CCCCN)C(=O)N[C@@]([H])(CS)C(=O)N[C@@]([H])(CCCNC(=N)N)C(=O)N[C@@]([H])(CCCNC(=N)N)C(=O)N[C@@]([H])(CC(=CN2)C1=C2C=CC=C1)C(=O)N[C@@]([H])(CCC(=O)N)C(=O)N[C@@]([H])(CC(=CN2)C1=C2C=CC=C1)C(=O)N[C@@]([H])(CCCNC(=N)N)C(=O)N[C@@]([H])(CCSC)C(=O)N[C@@]([H])(CCCCN)C(=O)N[C@@]([H])(CCCCN)C(=O)N[C@@]([H])(CC(C)C)C(=O)NCC(=O)N[C@@]([H])(C)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(CO)C(=O)N[C@@]([H])([C@]([H])(CC)C)C(=O)N[C@@]([H])([C@]([H])(O)C)C(=O)N[C@@]([H])(CS)C(=O)N[C@@]([H])(C(C)C)C(=O)N[C@@]([H])(CCCNC(=N)N)C(=O)O

Preparation method

Mode of preparation	Enzymatic hydrolysis
Enzyme(s)/starter culture	Pepsin hydrolysates of bovine lactoferrin showed a greater growth suppressive effect than tryptic hydrolysates or mature bovine lactoferrin, so the peptide was obtained by pepsin hydrolysis.

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	Roy, M.K., Kuwabara, Y., Hara, K., Watanabe, Y., Tamai, Y. Peptides From the N-terminal End of Bovine Lactoferrin Induce Apoptosis in Human Leukemic (HL-60) Cells. Journal of Dairy Science. 2002, 85, 2065-74. DOI: 10.3168/jds.S0022-0302(02)74284-7
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] Mader J S, Salsman J, Conrad D M, et al. Bovine lactoferricin selectively induces apoptosis in human leukemia and carcinoma cell lines.[J]. Molecular Cancer Therapeutics, 2005, 4(4):612.
PubDate	2002