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 - DFBPMIBP0017(Mineral-binding peptide)

DFBP ID	DFBPMIBP0017
Peptide sequence	NAPLPPPLKH
Type	Native peptide
Peptide/Function name	Mineral-binding petpide, Zinc-chelating peptide

Function-activity relationship

Main bioactivity	Mineral-binding activity
Otheir bioactivity	N.D

Calculated physicochemical properties

Three-letter amino acid

Asn-Ala-Pro-Leu-Pro-Pro-Pro-Leu-Lys-His

Single-letter amino acid

NAPLPPPLKH

Peptide length

Peptide mass

Experimental mass	Theoretical mass
1084 Da	1083.28 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

10.04 ^c

IC₅₀

N.D

pIC₅₀

N.D

GRAVY

-0.7600^c

Hydrophilic residue ratio

70%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Plant
Organism/Source	Wheat
Precursor protein	Defatted wheat germ protein
Residue position	N.D
Precursor protein(s) search	No matching precursor protein found
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

The peptide NAPLPPPLKH showed a relatively low zinc chelating capacity of 15.15 ± 0.70% compared with the peptide HNAPNPGLPYAA (91.67 ± 0.81%, P < 0.05).
The histidine residues at the N-terminal of the peptide may play important roles in the zinc-binding capacity. The zinc bioavailability estimated by Caco-2 cells after simulated gastrointestinal digestion of peptide–zinc complex was markedly higher when compared with inorganic Zn salt.

Table 1 – Zn binding capacity and Zn bioavailability of Zn-chelating peptides.
Materials	Zn binding capacity (%)	Zn bioavailability (%)
Fraction F22 of hydrolysates	86.78 ± 0.72^c	50.65 ± 0.42^b
NAPLPPPLKH	15.15 ± 0.70^a	—
HNAPNPGLPYAA	91.67 ± 0.81^b	51.26 ± 0.68^b
ZnSO₄	—	28.00 ± 1.22^a
Means ± SD (n = 3). Values followed by a different letter in the same column are significantly different at P < 0.05. – stands for not determined. The Zn bioavailability was tested in Caco-2 cells.

Specific target protein(s)

N.D

Taste properties & Structure

Bitterness

Literature report	N.D
Bitter prediction tools	Bitter taste ^prediction

SMILES

N[C@@]([H])(CC(=O)N)C(=O)N[C@@]([H])(C)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(CC(C)C)C(=O)N1[C@@]([H])(CCC1)C(=O)N1[C@@]([H])(CCC1)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(CC(C)C)C(=O)N[C@@]([H])(CCCCN)C(=O)N[C@@]([H])(CC1=CN=C-N1)C(=O)O

Preparation method

Mode of preparation	Enzymatic hydrolysis
Enzyme(s)/starter culture	The hydrolysates prepared by Alcalase under optimal conditions for 200 min had the highest degree of hydrolysis of 15.61 ± 0.09% and metal chelating ability of 69.62 ± 0.96%.

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

The results of this study suggest that wheat germ zinc-chelating peptides may be used as ingredients in functional foods or pharmaceutical preparations to increase the stability, absorption, and bioavailability of zinc.

Database cross-references

[D1]

[D2]

[D3]

[D4]

Reference(s)

Primary literature	Zhu, K.-X., Wang, X.-P., Guo, X.-N. Isolation and characterization of zinc-chelating peptides from wheat germ protein hydrolysates. Journal of Functional Foods. 2015, 12, 23-32. DOI: 10.1016/j.jff.2014.10.030
Other literature(s)	N.D
PubDate	2015