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 - DFBPMIBP0004(Mineral-binding peptide)

DFBP ID	DFBPMIBP0004
Peptide sequence	KNTMEHVSSSEESIISQETYKQEKNMAINPSK
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

Lys-Asn-Thr-Met-Glu-His-Val-Ser-Ser-Ser-Glu-Glu-Ser-Ile-Ile-Ser-Gln-Glu-Thr-Tyr-Lys-Gln-Glu-Lys-Asn-Met-Ala-Ile-Asn-Pro-Ser-Lys

Single-letter amino acid

KNTMEHVSSSEESIISQETYKQEKNMAINPSK

Peptide length

Peptide mass

Experimental mass	Theoretical mass
N.D	3669.03 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

5.58 ^c

IC₅₀

N.D

pIC₅₀

N.D

GRAVY

-1.2375^c

Hydrophilic residue ratio

25%^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(1-32)
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
KNTMEHVSSSEESIISQETYKQEKNMAINPSK	0	N.D	Ca, Fe
KNTMEHVΣΣΣEESIIΣQETYKQEKNMAINPSK	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

N[C@@]([H])(CCCCN)C(=O)N[C@@]([H])(CC(=O)N)C(=O)N[C@@]([H])([C@]([H])(O)C)C(=O)N[C@@]([H])(CCSC)C(=O)N[C@@]([H])(CCC(=O)O)C(=O)N[C@@]([H])(CC1=CN=C-N1)C(=O)N[C@@]([H])(C(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])(CC)C)C(=O)N[C@@]([H])(CO)C(=O)N[C@@]([H])(CCC(=O)N)C(=O)N[C@@]([H])(CCC(=O)O)C(=O)N[C@@]([H])([C@]([H])(O)C)C(=O)N[C@@]([H])(Cc1ccc(O)cc1)C(=O)N[C@@]([H])(CCCCN)C(=O)N[C@@]([H])(CCC(=O)N)C(=O)N[C@@]([H])(CCC(=O)O)C(=O)N[C@@]([H])(CCCCN)C(=O)N[C@@]([H])(CC(=O)N)C(=O)N[C@@]([H])(CCSC)C(=O)N[C@@]([H])(C)C(=O)N[C@@]([H])([C@]([H])(CC)C)C(=O)N[C@@]([H])(CC(=O)N)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(CO)C(=O)N[C@@]([H])(CCCCN)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]	DFBPIMMU0030
[D2]	DFBPMUFU0758

[D3]

[D4]

[D5]

[D6]

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