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 - DFBPALGL0003(α-Glucosidase inhibitory peptide)

DFBP ID	DFBPALGL0003
Peptide sequence	RVPSLM
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

Arg-Val-Pro-Ser-Leu-Met

Single-letter amino acid

RVPSLM

Peptide length

Peptide mass

Experimental mass	Theoretical mass
N.D	701.87 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

11.04 ^c

IC₅₀

N.D

pIC₅₀

N.D

GRAVY

0.5000^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	Ovotransferrin
Residue position	f(328-333)
Precursor protein(s) search	Source.1: DFBPPR9971 ---- Animal proteins ---- Ovotransferrin
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). RVPSLM was discovered as a potential α-glucosidase inhibitor with an IC₅₀ value at 23.07 umol/L. However, it did not exhibit a visible or detectable inhibitory efficiency on the α-amylase (IC₅₀ > 150.0 umol/L). This peptide could be considered as a potential AGI agent. For instance, the α-glucosidase inhibitory activity of RVPSLM was comparable to that of the therapeutic AGI drug acarbose (IC₅₀ 60.8 umol/L)^[1].

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])(CCCNC(=N)N)C(=O)N[C@@]([H])(C(C)C)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(CO)C(=O)N[C@@]([H])(CC(C)C)C(=O)N[C@@]([H])(CCSC)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]	DFBPANOX0621
[D2]	DFBPANTH0085
[D3]	DFBPALAM0012
[D4]	DFBPMUFU0671

[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)	[1] Seo W D, Kim J H, Kang J E, et al. Sulfonamide chalcone as a new class of alpha-glucosidase inhibitors[J]. Bioorganic & Medicinal Chemistry Letters, 2005, 15(24):5514-5516.
PubDate	2011