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 - DFBPANCA0007(Anticancer peptide)

DFBP ID	DFBPANCA0007
Peptide sequence	FKCRRWQWRMKKLGAPSITCVRRAF
Type	Native peptide
Peptide/Function name	Anticancer peptide, Lactoferricin B (LfcinB)

Function-activity relationship

Main bioactivity	Anticancer activity
Otheir bioactivity	Antimicrobial activity ^[D1], Immunomodulatory activity ^[D2], Multifunctional activity ^[D3]

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-Arg-Ala-Phe

Single-letter amino acid

FKCRRWQWRMKKLGAPSITCVRRAF

Peptide length

Peptide mass

Experimental mass	Theoretical mass
N.D	3125.80 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

12.34 ^c

IC₅₀

N.D

pIC₅₀

N.D

GRAVY

-0.5760^c

Hydrophilic residue ratio

48%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Animal
Organism/Source	Bovine milk
Precursor protein	Lactoferricin (LfcinB) peptide from bovine lactoferrin
Residue position	N.D
Precursor protein(s) search	Source.1: DFBPPR8500 ---- Milk proteins ---- Lactotransferrin
Link-research Inductive analysis	Link 1: DFBPANCA0055----Bovine milk----Lactoferrin (LF-B) Link 2: DFBPANCA0334----Bovine milk protein----Lactoferricin

Biological/Functional activity & target protein

Anticancer activity	Exhibited cytotoxic activity due to mitochondria (Jurkat T leukemia cells.). Disulfide bond is not required for the antimicrobial potency. Active against: Gram+ & Gram-, virus, fungi, cancer cells ^[2].
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)N[C@@]([H])(CCCNC(=N)N)C(=O)N[C@@]([H])(C)C(=O)N[C@@]([H])(Cc1ccccc1)C(=O)O

Preparation method

Mode of preparation	Enzymatic hydrolysis
Enzyme(s)/starter culture	Hydrolysis with pepsin.

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

DFBP

[D1]	DFBPAMIC0005
[D2]	DFBPIMMU0026
[D3]	DFBPMUFU0698

BIOPEP-UWM

[D4]

3229, 7051, 8175

APD

[D5]

BioPepDB

[D6]

MBPDB

[D7]

Reference(s)

Primary literature	Mader JS, Salsman J, Conrad DM, Hoskin DW. Bovine lactoferricin selectively induces apoptosis in human leukemia and carcinoma cell lines. Mol Cancer Ther. 2005 Apr;4(4):612-24. PMID: 15827335 DOI: 10.1158/1535-7163.MCT-04-0077
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] Peter M. Hwang,‡, Ning Zhou,‡, Xi Shan,§, et al. Three-Dimensional Solution Structure of Lactoferricin B, an Antimicrobial Peptide Derived from Bovine Lactoferrin†[J]. Biochemistry, 1998, 37(12):4288. [3] Mader J S, Richardson A, Salsman J, et al. Bovine lactoferricin causes apoptosis in Jurkat T-leukemia cells by sequential permeabilization of the cell membrane and targeting of mitochondria[J]. Experimental Cell Research, 2007, 313(12):2634-2650.
PubDate	2005