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 - DFBPMIBP0008(Mineral-binding peptide)

DFBP ID	DFBPMIBP0008
Peptide sequence	RELEELNVPGEIVESLSSSEESITR
Type	Native peptide
Peptide/Function name	Mineral-binding petpide, Caseinophosphopeptide

Function-activity relationship

Main bioactivity	Mineral-binding activity
Otheir bioactivity	Antithrombotic activity ^[D1], Immunomodulatory activity ^[D2], Multifunctional activity ^[D3]

Calculated physicochemical properties

Three-letter amino acid

Arg-Glu-Leu-Glu-Glu-Leu-Asn-Val-Pro-Gly-Glu-Ile-Val-Glu-Ser-Leu-Ser-Ser-Ser-Glu-Glu-Ser-Ile-Thr-Arg

Single-letter amino acid

RELEELNVPGEIVESLSSSEESITR

Peptide length

Peptide mass

Experimental mass	Theoretical mass
N.D	2802.98 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

3.92 ^c

IC₅₀

N.D

pIC₅₀

N.D

GRAVY

-0.5960^c

Hydrophilic residue ratio

36%^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(1-25)
Precursor protein(s) search	Source.1: 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
RELEELNVPGEIVESLSSSEESITR	0	N.D	Ca, Fe
RELEELNVPGEIVEΣLΣΣΣEESITR	4	-9	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])(CCCNC(=N)N)C(=O)N[C@@]([H])(CCC(=O)O)C(=O)N[C@@]([H])(CC(C)C)C(=O)N[C@@]([H])(CCC(=O)O)C(=O)N[C@@]([H])(CCC(=O)O)C(=O)N[C@@]([H])(CC(C)C)C(=O)N[C@@]([H])(CC(=O)N)C(=O)N[C@@]([H])(C(C)C)C(=O)N1[C@@]([H])(CCC1)C(=O)NCC(=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)N[C@@]([H])(CCC(=O)O)C(=O)N[C@@]([H])(CO)C(=O)N[C@@]([H])(CC(C)C)C(=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@]([H])(CC)C)C(=O)N[C@@]([H])([C@]([H])(O)C)C(=O)N[C@@]([H])(CCCNC(=N)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

DFBP

[D1]	DFBPANTH0132
[D2]	DFBPIMMU0044
[D3]	DFBPMUFU0723

[D4]

[D5]

[D6]

[D7]

Reference(s)

Primary literature	Sato R, Shindo M, Gunshin H, Noguchi T, Naito H. Characterization of phosphopeptide derived from bovine beta-casein: an inhibitor to intra-intestinal precipitation of calcium phosphate. Biochim Biophys Acta. 1991 Apr 29;1077(3):413-5. PMID: 2029541 DOI: 10.1016/0167-4838(91)90559-i
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] Reynolds E, Riley PF & Adamson N (1994) A selective precipitation purification procedure for multiple phophoseryl-containing peptides and methods for their identification. Journal of Analytical Biochemistry 217, 277-284. [3] Schlimme E & Meisel H (1995) Bioactive peptides derived from milk proteins: structural, physiological and analytical aspects. Die Nahrung 39, 1-20. [4] Gaucheron F, Famelart MH & Le Graet Y (1996) Iron-supplement caseins: preparation, physiochemical characterization and stability. Journal of Dairy Research 63, 233-243. [5] Meisel H & Schlimme E (1996) Bioactive peptides derived from milk proteins: ingredients for functional foods? Kieler Milchwirtschaftliche Forshungsberichte 48, 343-357. [6] Peres JM, Bouhallab S, Bureau F, Maubois JL, Arhan P & Bougle D (1997) Absorption digestive du fer lieau caseinophosphopeptide 1-25 de la b-caseine. Le Lait 77, 433-440. [7] H. M , J. F R . Biofunctional Peptides from Milk Proteins: Mineral Binding and Cytomodulatory Effects[J]. curr pharm des, 2003, 9(16):1289-1295. [8] Fitzgerald R J . Potential Uses of Caseinophosphopeptides[J]. International Dairy Journal, 1998, 8(5):451-457.
PubDate	1991