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 - DFBPMIBP0006(Mineral-binding peptide)

DFBP ID	DFBPMIBP0006
Peptide sequence	FQSEEQQQTEDELQDK
Type	Native peptide
Peptide/Function name	Mineral-binding petpide, Caseinophosphopeptide

Function-activity relationship

Main bioactivity	Mineral-binding activity
Otheir bioactivity	Antithrombotic activity ^[D1], Multifunctional activity ^[D2]

Calculated physicochemical properties

Three-letter amino acid

Phe-Gln-Ser-Glu-Glu-Gln-Gln-Gln-Thr-Glu-Asp-Glu-Leu-Gln-Asp-Lys

Single-letter amino acid

FQSEEQQQTEDELQDK

Peptide length

Peptide mass

Experimental mass	Theoretical mass
N.D	1982.00 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

3.49 ^c

IC₅₀

N.D

pIC₅₀

N.D

GRAVY

-2.3312^c

Hydrophilic residue ratio

12.5%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Animal
Organism/Source	Bovine milk protein (Casein-derived phosphopeptides)
Precursor protein	β-Casein
Residue position	f(33-48)
Precursor protein(s) search	Source.1: DFBPPR7692 ---- Milk proteins ---- Beta-casein Source.2: DFBPPR7700 ---- Milk proteins ---- Beta-casein Source.3: DFBPPR8489 ---- Milk proteins ---- Beta-casein
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

Mineral-binding activity

Peptide	Phosphoresidues	Net charge	Mineral binding
FQSEEQQQTEDELQDK	0	N.D	Ca
FQΣEEQQQTEDELQDK	1	-6	Ca
The one-letter amino acid codes were used; phosphoserine = Σ.

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])(Cc1ccccc1)C(=O)N[C@@]([H])(CCC(=O)N)C(=O)N[C@@]([H])(CO)C(=O)N[C@@]([H])(CCC(=O)O)C(=O)N[C@@]([H])(CCC(=O)O)C(=O)N[C@@]([H])(CCC(=O)N)C(=O)N[C@@]([H])(CCC(=O)N)C(=O)N[C@@]([H])(CCC(=O)N)C(=O)N[C@@]([H])([C@]([H])(O)C)C(=O)N[C@@]([H])(CCC(=O)O)C(=O)N[C@@]([H])(CC(=O)O)C(=O)N[C@@]([H])(CCC(=O)O)C(=O)N[C@@]([H])(CC(C)C)C(=O)N[C@@]([H])(CCC(=O)N)C(=O)N[C@@]([H])(CC(=O)O)C(=O)N[C@@]([H])(CCCCN)C(=O)O

Preparation method

Mode of preparation	Enzymatic hydrolysis
Enzyme(s)/starter culture	Bovine milk protein was hydrolyzed by trypsin.

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]	DFBPANTH0130, DFBPANTH0168
[D2]	DFBPMUFU0722

[D3]

[D4]

[D5]

[D6]

Reference(s)

Primary literature	Juillerat, M., Baechler, R., Berrocal, R., Chanton, S., Scherz, J.-C., Jost, R. Tryptic phosphopeptides from whole casein. I. Preparation and analysis by fast protein liquid chromatography. Journal of Dairy Research. 1989, 56, 603-11. DOI: 10.1017/S0022029900029125
Other literature(s)	[1] Vegarud G E, Langsrud T, Svenning C. Mineral-binding milk proteins and peptides; occurrence, biochemical and technological characteristics[J]. British Journal of Nutrition, 2000, 84(S1):S91---S98. [2] Meisel H & Schlimme E (1996) Bioactive peptides derived from milk proteins: ingredients for functional foods? Kieler Milchwirtschaftliche Forshungsberichte 48, 343-357. [3] H. M , J. F R . Biofunctional Peptides from Milk Proteins: Mineral Binding and Cytomodulatory Effects[J]. curr pharm des, 2003, 9(16):1289-1295. [4] Fitzgerald R J . Potential Uses of Caseinophosphopeptides[J]. International Dairy Journal, 1998, 8(5):451-457.
PubDate	1989