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 - DFBPDPIV0237(DPP IV-inhibitory peptide)

DFBP ID	DFBPDPIV0237
Peptide sequence	VLATSGPG
Type	Native peptide
Peptide/Function name	DPP-IV inhibitory peptide, Anti-diabetic peptide

Function-activity relationship

Main bioactivity	DPP-IV inhibitory activity
Otheir bioactivity	N.D

Calculated physicochemical properties

Three-letter amino acid

Val-Leu-Ala-Thr-Ser-Gly-Pro-Gly

Single-letter amino acid

VLATSGPG

Peptide length

Peptide mass

Experimental mass	Theoretical mass
N.D	700.78 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

5.97 ^c

IC₅₀

N.D

pIC₅₀

N.D

GRAVY

0.7375^c

Hydrophilic residue ratio

75%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Animal, Marine fish
Organism/Source	Salmon
Precursor protein	Salmon skin collagen
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

DPP IV-inhibitory activity	(1) The peptide VLATSGPG inhibited the Dipeptidyl-peptidase IV (EC 3.4.14.5) in the cells via a mixed-type inhibition mode, with in situ IC₅₀ values of 207.3 μM. (2) The VLATSGPG was transported intact across the cells, with P-app values of 2.41 ± 0.16 × 10^-7 cm/s.
Specific target protein(s)	Specific Target Protein(s): Dipeptidyl peptidase 4

Taste properties & Structure

Bitterness

Literature report	N.D
Bitter prediction tools	Non-bitter taste ^prediction

SMILES

N.D

Preparation method

Mode of preparation	Enzymatic hydrolysis
Enzyme(s)/starter culture	Salmon skin collagen was hydrolyzed by pepsin, trypsin, papain, or Alcalase 2.4 L, separately. Trypsin hydrolysate (10 mg/mL) showed the highest inhibitory activity of 66.12 ± 0.68% ^[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

This study demonstrates that this peptide potentially regulate DPP-IV activity in the intestine.

Database cross-references

[D1]

[D2]

[D3]

[D4]

Reference(s)

Primary literature	Jin R, Shang J, Teng X, Zhang L, Liao M, Kang J, Meng R, Wang D, Ren H, Liu N. Characterization of DPP-IV Inhibitory Peptides Using an In Vitro Cell Culture Model of the Intestine. J Agric Food Chem. 2021 Mar 10;69(9):2711-2718. PMID: 33629836 DOI: 10.1021/acs.jafc.0c05880
Other literature(s)	[1] Jin R, Teng X, Shang J, Wang D, Liu N. Identification of novel DPP-IV inhibitory peptides from Atlantic salmon (Salmo salar) skin. Food Res Int. 2020 Jul;133:109161. doi: 10.1016/j.foodres.2020.109161. Epub 2020 Mar 17. PMID: 32466942.
PubDate	2021