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 - DFBPIMMU0026(Immunomodulatory peptide)

DFBP ID	DFBPIMMU0026
Peptide sequence	FKCRRWQWRMKKLGAPSITCVRRAF
Type	Native peptide
Peptide/Function name	Immunomodulatory peptide, Lactoferricin B

Function-activity relationship

Main bioactivity	Immunomodulatory activity
Otheir bioactivity	Antimicrobial activity ^[D1], Anticancer 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
Precursor protein	Lactoferrin
Residue position	f(17-41)
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

Immunomodulatory activity	The peptide showed immunomodulatory activity.
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	Milk proteins were hydrolyzed 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]	DFBPANCA0007, DFBPANCA0055, DFBPANCA0334
[D3]	DFBPMUFU0698

BIOPEP-UWM

[D4]

3229, 7051, 8175

APD

[D5]

BioPepDB

[D6]

MBPDB

[D7]

Reference(s)

Primary literature	Bellamy W, Takase M, Wakabayashi H, Kawase K, Tomita M. Antibacterial spectrum of lactoferricin B, a potent bactericidal peptide derived from the N-terminal region of bovine lactoferrin. J Appl Bacteriol. 1992 Dec;73(6):472-9. PMID: 1490908 DOI: 10.1111/j.1365-2672.1992.tb05007.x
Other literature(s)	[1] Park Y W. Bioactive Components in Milk and Dairy Products[M]. 2009. [2] Hayes M, Ross RP, Fitzgerald GF, et al. Putting microbes to work: dairy fermentation, cell factories and bioactive peptides. Part II: Bioactive peptide functions[J]. Biotechnology Journal, 2007, 2(4):435–449. [3] Miyauchi H, Hashimoto S, Nakajima M, et al. Bovine lactoferrin stimulates the phagocytic activity of human neutrophils: identification of its active domain[J]. Cellular Immunology, 1998, 187(1):34-7.
PubDate	1992