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 - DFBPDPIV0025(DPP IV-inhibitory peptide)

DFBP ID	DFBPDPIV0025
Peptide sequence	VAGTWY
Type	Native peptide
Peptide/Function name	DPP-IV inhibitory peptide, Anti-diabetic peptide

Function-activity relationship

Main bioactivity	DPP-IV inhibitory activity
Otheir bioactivity	ACE-inhibitory activity ^[D1], Antioxidative activity ^[D2], Antimicrobial activity ^[D3], Multifunctional activity ^[D4]

Calculated physicochemical properties

Three-letter amino acid

Val-Ala-Gly-Thr-Trp-Tyr

Single-letter amino acid

VAGTWY

Peptide length

Peptide mass

Experimental mass	Theoretical mass
N.D	695.77 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

5.92 ^c

IC₅₀

N.D

pIC₅₀

N.D

GRAVY

0.4500^c

Hydrophilic residue ratio

66.67%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Milk proteins
Organism/Source	Bovine, Whey protein
Precursor protein	β-Lactoglobulin
Residue position	f(15-20)
Precursor protein(s) search	Source.1: DFBPPR7687 ---- Milk proteins ---- Beta-lactoglobulin Source.2: DFBPPR7714 ---- Milk proteins ---- Beta-lactoglobulin Source.3: DFBPPR8499 ---- Milk proteins ---- Beta-lactoglobulin
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) Inhibitor of Dipeptidyl-peptidase IV (EC 3.4.14.5). The peptide VAGTWY showed notable inhibitory activity with IC₅₀ values of 174.0 μM. (2) The IC₅₀ value was 74.9 ± 4.4 μM ^[1].
Specific target protein(s)	Specific Target Protein(s): Dipeptidyl peptidase 4

Taste properties & Structure

Bitterness

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

SMILES

N[C@@]([H])(C(C)C)C(=O)N[C@@]([H])(C)C(=O)NCC(=O)N[C@@]([H])([C@]([H])(O)C)C(=O)N[C@@]([H])(CC(=CN2)C1=C2C=CC=C1)C(=O)N[C@@]([H])(Cc1ccc(O)cc1)C(=O)O

Preparation method

Mode of preparation	Enzymatic hydrolysis
Enzyme(s)/starter culture	The whey protein concentrate rich in β-lactoglobulin was hydrolysed with trypsin and the trypsin was added at an enzyme-to-substrate ratio of 1:20 (w/w) and hydrolysis was carried out at 37 ℃ for 3 h with constant agitation.

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

β-Lactoglobulin derived peptides may form part of a functional food based dietary strategy for the management of CVD and T2DM ^[1].

Database cross-references

DFBP

[D1]	DFBPACEI0361
[D2]	DFBPANOX0699
[D3]	DFBPAMIC0336
[D4]	DFBPMUFU0111

BIOPEP-UWM

[D5]

3509, 4014, 8498, 8523, 9435

APD

[D6]

BioPepDB

[D7]

MBPDB

[D8]

Reference(s)

Primary literature	Silveira ST, Martínez-Maqueda D, Recio I, Hernández-Ledesma B. Dipeptidyl peptidase-IV inhibitory peptides generated by tryptic hydrolysis of a whey protein concentrate rich in β-lactoglobulin. Food Chem. 2013 Nov 15;141(2):1072-7. PMID: 23790888 DOI: 10.1016/j.foodchem.2013.03.056
Other literature(s)	[1] Power O, Fernández A, Norris R, et al. Selective enrichment of bioactive properties during ultrafiltration of a tryptic digest of β-lactoglobulin[J]. Journal of Functional Foods, 2014, 9:38-47. [2] Uchida M, Ohshiba Y, Mogami O. Novel dipeptidyl peptidase-4-inhibiting peptide derived from β-lactoglobulin[J]. Journal of Pharmacological Sciences, 2011, 117(1):63. [3] Pellegrini A, Dettling C, Thomas U, et al. Isolation and characterization of four bactericidal domains in the bovine β-lactoglobulin[J]. Biochimica Et Biophysica Acta General Subjects, 2001, 1526(2):131-140. [4] Lacroix I M E, Li-Chan E C Y. Evaluation of the potential of dietary proteins as precursors of dipeptidyl peptidase (DPP)-IV inhibitors by an in silico, approach[J]. Journal of Functional Foods, 2012, 4(2):403-422.
PubDate	2013