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 - DFBPMIBP0007(Mineral-binding peptide)

DFBP ID	DFBPMIBP0007
Peptide sequence	RELEELNVPGEIVESLSSSEESITRINK
Type	Native peptide
Peptide/Function name	Mineral-binding petpide, Caseinophosphopeptide

Function-activity relationship

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

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-Ile-Asn-Lys

Single-letter amino acid

RELEELNVPGEIVESLSSSEESITRINK

Peptide length

Peptide mass

Experimental mass	Theoretical mass
N.D	3158.42 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

4.20 ^c

IC₅₀

N.D

pIC₅₀

N.D

GRAVY

-0.6357^c

Hydrophilic residue ratio

35.71%^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(1-28)
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
RELEELNVPGEIVESLSSSEESITRINK	0	N.D	Ca
RELEELNVPGEIVEΣLΣΣΣEESITRINK	4	-8	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])(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)N[C@@]([H])([C@]([H])(CC)C)C(=O)N[C@@]([H])(CC(=O)N)C(=O)N[C@@]([H])(CCCCN)C(=O)O

Structure

Embedded Mol* Viewer

Docking

Embedded Mol* Viewer

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]	DFBPIMMU0031
[D2]	DFBPMUFU0759

[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] Chung TDY & Raymond KN (1993) Lactoferrin: the role of conformational changes in its iron binding and release. Journal of American Chemical Society 115, 6765-6768. [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