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 - DFBPMIBP0003(Mineral-binding peptide)

DFBP ID	DFBPMIBP0003
Peptide sequence	DIGSESTEDQAMEDIM
Type	Native peptide
Peptide/Function name	Mineral-binding petpide, Caseinophosphopeptide

Function-activity relationship

Main bioactivity	Mineral-binding activity
Otheir bioactivity	N.D

Calculated physicochemical properties

Three-letter amino acid

Asp-Ile-Gly-Ser-Glu-Ser-Thr-Glu-Asp-Gln-Ala-Met-Glu-Asp-Ile-Met

Single-letter amino acid

DIGSESTEDQAMEDIM

Peptide length

Peptide mass

Experimental mass	Theoretical mass
N.D	1770.83 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

2.76 ^c

IC₅₀

N.D

pIC₅₀

N.D

GRAVY

-0.7875^c

Hydrophilic residue ratio

37.5%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Animal
Organism/Source	Bovine milk protein (Casein-derived phosphopeptides)
Precursor protein	α_s1-Casein
Residue position	f(43-58)
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

Mineral-binding activity

Peptide	Phosphoresidues	Net charge	Mineral binding
DIGSESTEDQAMEDIM	0	N.D	Ca, Fe
DIGΣEΣTEDQAMEDIM	2	-7	Ca, Fe
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])(CC(=O)O)C(=O)N[C@@]([H])([C@]([H])(CC)C)C(=O)NCC(=O)N[C@@]([H])(CO)C(=O)N[C@@]([H])(CCC(=O)O)C(=O)N[C@@]([H])(CO)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)N)C(=O)N[C@@]([H])(C)C(=O)N[C@@]([H])(CCSC)C(=O)N[C@@]([H])(CCC(=O)O)C(=O)N[C@@]([H])(CC(=O)O)C(=O)N[C@@]([H])([C@]([H])(CC)C)C(=O)N[C@@]([H])(CCSC)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

[D1]

[D2]

[D3]

[D4]

Reference(s)

Primary literature	Meisel, H., Schlimme, E. Bindungsvermogen fur Calcium und Eisen verschiedener Fractionen aus der in vitro-proteolyse von Casein. Kieler Milchwirtschaftliche Forshungsberichte. 1993, 45, 235-243.
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] Juillerat M, Baechler R, Berrocal R, Chanton S, Scherz JC & Jost R (1989) Tryptic phosphopeptide from whole casein. 1. Preparation and analysis by fast protein liquid chromatography. Journal of Dairy Research 56, 603-611. [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.
PubDate	1993