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 - DFBPMIBP0001(Mineral-binding peptide)

DFBP ID	DFBPMIBP0001
Peptide sequence	SSSEEIVPN
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

Ser-Ser-Ser-Glu-Glu-Ile-Val-Pro-Asn

Single-letter amino acid

SSSEEIVPN

Peptide length

Peptide mass

Experimental mass	Theoretical mass
N.D	960.98 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

3.19 ^c

IC₅₀

N.D

pIC₅₀

N.D

GRAVY

-0.6444^c

Hydrophilic residue ratio

33.33%^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(66-74)
Precursor protein(s) search	Source.1: DFBPPR7688 ---- Milk proteins ---- Alpha-S1-casein Source.2: DFBPPR7694 ---- Milk proteins ---- Alpha-S1-casein Source.3: DFBPPR8488 ---- Milk proteins ---- Alpha-S1-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
SSSEEIVPN	0	N.D	Ca, Fe
ΣΣΣEEIVPN	3	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

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])([C@]([H])(CC)C)C(=O)N[C@@]([H])(C(C)C)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(CC(=O)N)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	Schlimme E, Meisel H. Bioactive peptides derived from milk proteins. Structural, physiological and analytical aspects. Nahrung. 1995;39(1):1-20. PMID: 7898574 DOI: 10.1002/food.19950390102
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] Zhang P & Allan J (1995) Free zinc concentration in bovine milk measurements by analytical affinity chromatography with immobilised metallothionein. Biological Trace Elements Research 50, 135-148. [3] Meisel H & Schlimme E (1996) Bioactive peptides derived from milk proteins: ingredients for functional foods? Kieler Milchwirtschaftliche Forshungsberichte 48, 343-357.
PubDate	1995