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 - DFBPALGL0008(α-Glucosidase inhibitory peptide)

DFBP ID	DFBPALGL0008
Peptide sequence	DHPFLF
Type	Native peptide
Peptide/Function name	α-Glucosidase inhibitory peptide, Anti-diabetic peptide

Function-activity relationship

Main bioactivity	α-Glucosidase inhibitory activity
Otheir bioactivity	Antioxidative activity ^[D1], Antithrombotic activity ^[D2], α-Amylase inhibitory activity ^[D3], Multifunctional activity ^[D4]

Calculated physicochemical properties

Three-letter amino acid

Asp-His-Pro-Phe-Leu-Phe

Single-letter amino acid

DHPFLF

Peptide length

Peptide mass

Experimental mass	Theoretical mass
N.D	774.86 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

4.96 ^c

IC₅₀

N.D

pIC₅₀

N.D

GRAVY

0.1833^c

Hydrophilic residue ratio

66.67%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Animal
Organism/Source	Egg white protein
Precursor protein	Ovalbumin (386AA)
Residue position	f(362-367)
Precursor protein(s) search	Source.1: DFBPPR3950 ---- Plant proteins ---- Serpin-ZXA Source.2: DFBPPR4055 ---- Plant proteins ---- Serpin-ZXB Source.3: DFBPPR6781 ---- Plant proteins ---- Serpin-Z1A Source.4: DFBPPR6797 ---- Plant proteins ---- Serpin-Z2B Source.5: DFBPPR6799 ---- Plant proteins ---- Serpin-Z1B Source.6: DFBPPR6818 ---- Plant proteins ---- Serpin-Z2A Source.7: DFBPPR6820 ---- Plant proteins ---- Serpin-Z1C Source.8: DFBPPR7147 ---- Plant proteins ---- Serpin-ZX Source.9: DFBPPR21779 ---- Animal proteins ---- Serpin B8 Source.10: DFBPPR21871 ---- Animal proteins ---- Serpin B10 Source.11: DFBPPR9993 ---- Animal proteins ---- Ovalbumin Source.12: DFBPPR10950 ---- Animal proteins ---- Ovalbumin-related protein Y Source.13: DFBPPR11500 ---- Animal proteins ---- Ovalbumin-related protein X
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-Glucosidase inhibitory activity

Inhibitor of α-Glucosidase (AGI, EC 3.2.1.20). The peptide did not exhibit visible or detectable inhibitory effect on the α-glucosidase (IC₅₀ > 150.0 umol/L) and α-amylase (IC₅₀ > 150.0 umol/L).

Table 1 α-Glucosidase and α-amylase inhibitory activities of the synthetic peptides
Peptide sequences	α-Glucosidase inhibitory activity (IC₅₀)	α-amylase inhibitory activity (IC₅₀)
RVPSLM	23.07 μmol/l	> 150.0 μmol/l
TPSPR	40.02 μmol/l	> 150.0 μmol/l
DLQGK	> 150.0 μmol/l	> 150.0 μmol/l
AGLAPY	> 150.0 μmol/l	> 150.0 μmol/l
RVPSL	> 150.0 μmol/l	> 150.0 μmol/l
DHPFLF	> 150.0 μmol/l	> 150.0 μmol/l
HAEIN	> 150.0 μmol/l	> 150.0 μmol/l
QIGLF	> 150.0 μmol/l	> 150.0 μmol/l

Specific target protein(s)

Specific Target Protein(s):
Lysosomal alpha-glucosidase

Taste properties & Structure

Bitterness

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

SMILES

N[C@@]([H])(CC(=O)O)C(=O)N[C@@]([H])(CC1=CN=C-N1)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(Cc1ccccc1)C(=O)N[C@@]([H])(CC(C)C)C(=O)N[C@@]([H])(Cc1ccccc1)C(=O)O

Preparation method

Mode of preparation	Enzymatic hydrolysis
Enzyme(s)/starter culture	The alkaline proteinase Alcalase was added to initiate the protein enzymatic hydrolysis.

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]	DFBPANOX0625
[D2]	DFBPANTH0089
[D3]	DFBPALAM0017
[D4]	DFBPMUFU0675

[D5]

[D6]

[D7]

[D8]

Reference(s)

Primary literature	Yu, Z., Yin, Y., Zhao, W., Yu, Y., Liu, B., Liu, J., et al. Novel peptides derived from egg white protein inhibiting alpha-glucosidase. Food Chem. 2011, 129, 1376-82. DOI: 10.1016/j.foodchem.2011.05.067
Other literature(s)	N.D
PubDate	2011