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 - DFBPAGPE0008(Alpha-gliadin peptide)

DFBP ID	DFBPAGPE0008
Peptide sequence	SQQQQPPFSQQQQPPFSQQQQPPFSQQQPPF
Type	Native peptide
Peptide/Function name	α-Gliadin peptide, Wheat allergenic peptide

Function-activity relationship

Main bioactivity	Wheat allergenic activity
Otheir bioactivity	N.D

Calculated physicochemical properties

Three-letter amino acid

Ser-Gln-Gln-Gln-Gln-Pro-Pro-Phe-Ser-Gln-Gln-Gln-Gln-Pro-Pro-Phe-Ser-Gln-Gln-Gln-Gln-Pro-Pro-Phe-Ser-Gln-Gln-Gln-Pro-Pro-Phe

Single-letter amino acid

SQQQQPPFSQQQQPPFSQQQQPPFSQQQPPF

Peptide length

Peptide mass

Experimental mass	Theoretical mass
3653.9290 Da	3653.95 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

5.97 ^c

IC₅₀

N.D

pIC₅₀

N.D

GRAVY

-1.8484^c

Hydrophilic residue ratio

38.71%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Plant
Organism/Source	Wheat
Precursor protein	Wheat gluten
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

Coeliac toxic activity

The peptide SQQQQPPFSQQQQPPFSQQQQPPFSQQQPPF was a major wheat allergenic tridecapeptide. The minimum epitope structure of the IgE-binding site for this peptide is Gln-Gln-Gln-Pro-Pro in which the N-terminal glutamine residue and the two proline residues are essential for binding. The author concluded that the Gln-Gln-Gln-Pro-Pro motif constituted an IgE-binding rather than immunogenic epitope and also that acetyl-Gln-Gln-Gln-Pro-Pro might act as a hapten capable of binding to specific IgE molecules.

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])(CCC(=O)N)C(=O)N[C@@]([H])(CCC(=O)N)C(=O)N[C@@]([H])(CCC(=O)N)C(=O)N[C@@]([H])(CCC(=O)N)C(=O)N1[C@@]([H])(CCC1)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(Cc1ccccc1)C(=O)N[C@@]([H])(CO)C(=O)N[C@@]([H])(CCC(=O)N)C(=O)N[C@@]([H])(CCC(=O)N)C(=O)N[C@@]([H])(CCC(=O)N)C(=O)N[C@@]([H])(CCC(=O)N)C(=O)N1[C@@]([H])(CCC1)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(Cc1ccccc1)C(=O)N[C@@]([H])(CO)C(=O)N[C@@]([H])(CCC(=O)N)C(=O)N[C@@]([H])(CCC(=O)N)C(=O)N[C@@]([H])(CCC(=O)N)C(=O)N[C@@]([H])(CCC(=O)N)C(=O)N1[C@@]([H])(CCC1)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(Cc1ccccc1)C(=O)N[C@@]([H])(CO)C(=O)N[C@@]([H])(CCC(=O)N)C(=O)N[C@@]([H])(CCC(=O)N)C(=O)N[C@@]([H])(CCC(=O)N)C(=O)N1[C@@]([H])(CCC1)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(Cc1ccccc1)C(=O)O

Preparation method

Mode of preparation	Enzymatic hydrolysis
Enzyme(s)/starter culture	The allergenic peptide was isolated from the chymotryptic hydrolysate of gluten^[1].

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	Tanabe S, Arai S, Yanagihara Y, Mita H, Takahashi K, Watanabe M. A major wheat allergen has a Gln-Gln-Gln-Pro-Pro motif identified as an IgE-binding epitope. Biochem Biophys Res Commun. 1996 Feb 15;219(2):290-3. PMID: 8604979 DOI: 10.1006/bbrc.1996.0225
Other literature(s)	[1] Watanabe M, Tanabe S, Suzuki T, et al. Primary structure of an allergenic peptide occurring in the chymotryptic hydrolysate of gluten[J]. Journal of the Agricultural Chemical Society of Japan, 1995, 59(8):1596-1597.
PubDate	1996