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 - DFBPALGL0043(α-Glucosidase inhibitory peptide)

DFBP ID	DFBPALGL0043
Peptide sequence	KVIISAPSKDAPMF
Type	Native peptide
Peptide/Function name	α-Glucosidase inhibitory peptide, Anti-diabetic peptide

Function-activity relationship

Main bioactivity	α-Glucosidase inhibitory activity
Otheir bioactivity	N.D

Calculated physicochemical properties

Three-letter amino acid

Lys-Val-Ile-Ile-Ser-Ala-Pro-Ser-Lys-Asp-Ala-Pro-Met-Phe

Single-letter amino acid

KVIISAPSKDAPMF

Peptide length

Peptide mass

Experimental mass	Theoretical mass
1502.817 Da	1503.79 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

9.84 ^c

IC₅₀

N.D

pIC₅₀

N.D

GRAVY

0.3857^c

Hydrophilic residue ratio

64.29%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Plant
Organism/Source	Changii Radix
Precursor protein	Glyceraldehyde-3-phosphate dehydrogenase (GAPDH)
Residue position	N.D
Precursor protein(s) search	Source.1: DFBPPR6329 ---- Plant proteins ---- Glyceraldehyde-3-phosphate dehydrogenase, cytosolic Source.2: DFBPPR7120 ---- Plant proteins ---- Glyceraldehyde-3-phosphate dehydrogenase 2, cytosolic
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	The peptide KVIISAPSKDAPMF exhibited potent α-Glucosidase (AGH, EC 3.2.1.20) inhibitory activity with an IC₅₀ value of 0.032 ± 0.099 mg/ mL.
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.D

Preparation method

Mode of preparation	Enzymatic hydrolysis
Enzyme(s)/starter culture	Among enzymatic hydrolysis conditions of trypsin, flavourzyme, compound proteinase, papain, alkaline proteinase, neutral protease, and in vitro simulated human gastrointestinal digestive conditions, the hydrolysate produced by simulated gastrointestinal digestion (pepsin + trypsin) showed the highest activity with an IC₅₀ vaule of 0.22 mg/mL.

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

Changii Radix derived peptides may have potential functions in the prevention and management of type 2 diabetes.

Database cross-references

[D1]

[D2]

[D3]

[D4]

Reference(s)

Primary literature	Bu, F.; Yi, D.; Zhang, H.; Li, Q.; Pan, D.; Dang, Y., Isolation and identification of antioxidant and DPP-IV inhibitory peptide PYPYEPYEPYPY from yak bone hydrolysate. Food Sci. Technol. Res. 2021,27 (3), 441-452. DOI: 10.1016/j.procbio.2021.08.019
Other literature(s)	N.D
PubDate	2021