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 - DFBPMIBP0005(Mineral-binding peptide)

DFBP ID	DFBPMIBP0005
Peptide sequence	GSSSEESAEV
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

Gly-Ser-Ser-Ser-Glu-Glu-Ser-Ala-Glu-Val

Single-letter amino acid

GSSSEESAEV

Peptide length

Peptide mass

Experimental mass	Theoretical mass
N.D	980.92 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

3.08 ^c

IC₅₀

N.D

pIC₅₀

N.D

GRAVY

-0.8100^c

Hydrophilic residue ratio

30%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Animal
Organism/Source	Bovine milk protein (Casein-derived phosphopeptides)
Precursor protein	α_s2-Casein
Residue position	f(55-64)
Precursor protein(s) search	Source.1: DFBPPR8494 ---- Milk proteins ---- Alpha-S2-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
GSSSEESAEV	0	N.D	Ca, Fe
GΣΣΣEEΣAEV	4	N.D	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

NCC(=O)N[C@@]([H])(CO)C(=O)N[C@@]([H])(CO)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])(CO)C(=O)N[C@@]([H])(C)C(=O)N[C@@]([H])(CCC(=O)O)C(=O)N[C@@]([H])(C(C)C)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	FitzGerald, R.J. Potential Uses of Caseinophosphopeptides. International Dairy Journal. 1998, 8, 451-7. DOI: 10.1016/S0958-6946(98)00068-5
Other literature(s)	[1] 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	1998