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 - DFBPALAM0008(α-Amylase inhibitory peptide)

DFBP ID	DFBPALAM0008
Peptide sequence	EAGVD
Type	Native peptide
Peptide/Function name	α-amylase inhibitory peptide, Anti-diabetic peptide

Function-activity relationship

Main bioactivity	Alpha-amylase inhibitory activity
Otheir bioactivity	α-Glucosidase inhibitory activity ^[D1], Multifunctional activity ^[D2]

Calculated physicochemical properties

Three-letter amino acid

Glu-Ala-Gly-Val-Asp

Single-letter amino acid

EAGVD

Peptide length

Peptide mass

Experimental mass	Theoretical mass
489.1959 Da	489.48 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

3.04 ^c

IC₅₀

N.D

pIC₅₀

N.D

GRAVY

-0.2800^c

Hydrophilic residue ratio

60%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Animal
Organism/Source	Egg White protein
Precursor protein	Albumin
Residue position	N.D
Precursor protein(s) search	Source.1: DFBPPR4569 ---- Plant proteins ---- Probable protein ABIL5 Source.2: DFBPPR5391 ---- Plant proteins ---- Glutathione S-transferase 4 Source.3: DFBPPR6826 ---- Plant proteins ---- Beta-amylase Tri a 17 Source.4: DFBPPR7043 ---- Plant proteins ---- Beta-amylase Source.5: DFBPPR19874 ---- Animal proteins ---- Cyclin-dependent kinase 4 inhibitor B Source.6: DFBPPR20156 ---- Animal proteins ---- Peptidyl-prolyl cis-trans isomerase FKBP9 Source.7: DFBPPR9988 ---- Animal proteins ---- Vinculin Source.8: DFBPPR9993 ---- Animal proteins ---- Ovalbumin Source.9: DFBPPR14882 ---- Microorganism protein ---- ATP-dependent 6-phosphofructokinase subunit beta
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

α-Amylase inhibitory activity	Inhibitor of alpha-amylase (EC 3.2.1.1). The peptide EAGVD had α-glucosidase inhibitory activity with an IC₅₀ of > 150.0 umol/l and α-amylase inhibitory activity with an IC50 of110.0 ± 6.2 umol/l, the results revealed that the peptide EAGVD was a potential anti-diabetic inhibitor.
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])(CCC(=O)O)C(=O)N[C@@]([H])(C)C(=O)NCC(=O)N[C@@]([H])(C(C)C)C(=O)N[C@@]([H])(CC(=O)O)C(=O)O

Preparation method

Mode of preparation	Enzymatic hydrolysis
Enzyme(s)/starter culture	The alkaline proteinase Alcalase was added at 4.0% of protein (w/w) for digestion.

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]	DFBPALGL0015
[D2]	DFBPMUFU0747

[D3]

[D4]

[D5]

[D6]

Reference(s)

Primary literature	Yu Z, Yin Y, Zhao W, Liu J, Chen F. Anti-diabetic activity peptides from albumin against α-glucosidase and α-amylase. Food Chem. 2012 Dec 1;135(3):2078-85. PMID: 22953959 DOI: 10.1016/j.foodchem.2012.06.088
Other literature(s)	[1] Yu Z, Yin Y, Zhao W, et al. Novel peptides derived from egg white protein inhibiting alpha-glucosidase[J]. Food Chemistry, 2011, 129(4):1376-1382.
PubDate	2012