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List of peptide properties
DFBP ID - DFBPDPIV0040(DPP IV-inhibitory peptide)
DFBP ID DFBPDPIV0040
Peptide sequence YPYY
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], Antihypertensive activity [D2], Antioxidative activity [D3], Opioid activity [D4], Multifunctional activity [D5]
Calculated physicochemical properties
Three-letter amino acid Tyr-Pro-Tyr-Tyr
Single-letter amino acid YPYY
Peptide length 4
Peptide mass
Experimental mass Theoretical mass
N.D 604.65 Da c
Net charge 0.00 c
Isoelectric point (pI) 5.83 c
IC50 N.D
pIC50 N.D
GRAVY -1.3750 c
Hydrophilic residue ratio 25% c
Peptide calculator
To calculate the physicochemical properties of bioactive peptide.
Peptide source & Food-borne protein(s) search
Classification Animal
Organism/Source Bovine milk protein
Precursor protein κ-Casein
Residue position

f(58-61)

Precursor protein(s) search
Source.1: DFBPPR1068 ---- Plant proteins ---- E3 ubiquitin-protein ligase DIS1
Source.2: DFBPPR2330 ---- Plant proteins ---- Probable staphylococcal-like nuclease CAN3
Source.3: DFBPPR2351 ---- Plant proteins ---- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit
Source.4: DFBPPR2528 ---- Plant proteins ---- Probable staphylococcal-like nuclease CAN2
Source.5: DFBPPR7608 ---- Milk proteins ---- Kappa-casein
Source.6: DFBPPR7686 ---- Milk proteins ---- Kappa-casein
Source.7: DFBPPR7695 ---- Milk proteins ---- Kappa-casein
Source.8: DFBPPR7715 ---- Milk proteins ---- Kappa-casein
Source.9: DFBPPR8492 ---- Milk proteins ---- Kappa-casein
Source.10: DFBPPR16086 ---- Animal proteins ---- Sodium/potassium-transporting ATPase subunit beta-1
Source.11: DFBPPR16300 ---- Animal proteins ---- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit
Source.12: DFBPPR16581 ---- Animal proteins ---- NADH-ubiquinone oxidoreductase chain 5
Source.13: DFBPPR17095 ---- Animal proteins ---- Hyaluronidase-1
Source.14: DFBPPR18973 ---- Animal proteins ---- Transcriptional activator Myb
Source.15: DFBPPR20798 ---- Animal proteins ---- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit
Source.16: DFBPPR21306 ---- Animal proteins ---- Protein ATP1B4
Source.17: DFBPPR8538 ---- Animal proteins ---- Sodium/potassium-transporting ATPase subunit beta-1
Source.18: DFBPPR8745 ---- Animal proteins ---- Hyaluronidase-1
Source.19: DFBPPR9339 ---- Animal proteins ---- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit
Source.20: DFBPPR9387 ---- Animal proteins ---- Protein ATP1B4
Source.21: DFBPPR10119 ---- Animal proteins ---- Down syndrome cell adhesion molecule homolog
Source.22: DFBPPR10355 ---- Animal proteins ---- Down syndrome cell adhesion molecule-like protein 1 homolog
Source.23: DFBPPR10358 ---- Animal proteins ---- Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase
Source.24: DFBPPR10687 ---- Animal proteins ---- Transcriptional activator Myb
Source.25: DFBPPR10752 ---- Animal proteins ---- Protein ATP1B4
Source.26: DFBPPR10897 ---- Animal proteins ---- Doublesex- and mab-3-related transcription factor 1
Source.27: DFBPPR11078 ---- Animal proteins ---- Sodium/potassium-transporting ATPase subunit beta-1
Source.28: DFBPPR11612 ---- Animal proteins ---- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit
Source.29: DFBPPR12562 ---- Animal proteins ---- Sodium/potassium-transporting ATPase subunit beta-1
Source.30: DFBPPR13549 ---- Animal proteins ---- Sodium/potassium-transporting ATPase subunit beta-1
Source.31: DFBPPR14863 ---- Marine protein ---- Sodium/potassium-transporting ATPase subunit beta-233
Source.32: DFBPPR14868 ---- Marine protein ---- Sodium/potassium-transporting ATPase subunit beta-1
Link-research
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

The peptide showed potent inhibitory activity for Dipeptidyl-peptidase IV (EC 3.4.14.5) with the IC50 value of 194.4 ± 13.0 μM (p = 0.05). The peptide displayed a substrate-type of inhibition towards DPP-IV. Its DPP-IV inhibitory pattern was shown by Lineweaver–Burk plots to be a competitive inhibition pattern [2].

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])(Cc1ccc(O)cc1)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(Cc1ccc(O)cc1)C(=O)N[C@@]([H])(Cc1ccc(O)cc1)C(=O)O
Preparation method
Mode of preparation

Enzymatic hydrolysis

Enzyme(s)/starter culture

In silico digestion of individual milk proteins was carried out with the peptide cutter program (ExPASy, 2011) using gastrointestinal enzymes (pepsin, trypsin and chymotrypsin).

Stability & Cytotoxicity
Peptide stability
Literature report:
Table 1 Concentration of milk protein-derived peptides inducing 50% inhibition (IC50) of dipeptidyl peptidase IV (DPP-IV) pre- (control) and post-hydrolysis of the milk protein-derived peptides with DPP-IV following incubation at 37 °C for 18 h at a low (1 U: 1 g peptide) and high (10 U: 1 g peptide) enzyme to substrate ratio (E:S).
Compound
DPP-IV IC50*
Control
Low E:S
High E:S
YPYY
207.9 ± 9.2 g,h
238.3 ± 48.1 h,i
523.4 ± 31.9 k
* Values represent mean IC50 values ± confidence interval (P = 0.05), n = 3. Values with different superscript letters are significantly different (P < 0.05).

EHP-Tool: Enzymatic Hydrolysis Prediction Tool (EHP-Tool)
Peptide cytotoxicity
Literature report: N.D
Prediction: ToxinPred
Additional information
Additional information

The results presented herein are relevant to the management of type 2 diabetes with functional foods involving multi-target sites for DPP-IV inhibition in humans.

Database cross-references
DFBP
[D1] DFBPACEI1213
[D2] DFBPANHY0564
[D3] DFBPANOX0680
[D4] DFBPOPIO0015, DFBPOPIO0128
[D5] DFBPMUFU0253
BIOPEP-UWM [D6] 3218, 8615
APD [D7] -
BioPepDB [D8] -
MBPDB [D9] -
Reference(s)
Primary literature Nongonierma AB, FitzGerald RJ. Susceptibility of milk protein-derived peptides to dipeptidyl peptidase IV (DPP-IV) hydrolysis. Food Chem. 2014 Feb 15;145:845-52.
PMID: 24128555
Other literature(s)

[1] Nongonierma A B, Fitzgerald R J. An in silico model to predict the potential of dietary proteins as sources of dipeptidyl peptidase IV (DPP-IV) inhibitory peptides[J]. Food Chemistry, 2014, 165(20):489-498.
[2] Nongonierma A B, Fitzgerald R J. Structure activity relationship modelling of milk protein-derived peptides with dipeptidyl peptidase IV (DPP-IV) inhibitory activity[J]. Peptides, 2016, 79:1-7.

PubDate 2014
Copyright © 2020. Record / license number: Chongqing ICP No. 2000214