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 - DFBPDPIV0223(DPP IV-inhibitory peptide)

DFBP ID	DFBPDPIV0223
Peptide sequence	YPWTQ
Type	Native peptide
Peptide/Function name	DPP-IV inhibitory peptide, Anti-diabetic peptide, Hemorphin-5, H5

Function-activity relationship

Main bioactivity	DPP-IV inhibitory activity
Otheir bioactivity	Opioid activity ^[D1], Multifunctional activity ^[D2]

Calculated physicochemical properties

Three-letter amino acid

Tyr-Pro-Trp-Thr-Gln

Single-letter amino acid

YPWTQ

Peptide length

Peptide mass

Experimental mass	Theoretical mass
N.D	693.76 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

5.92 ^c

IC₅₀

N.D

pIC₅₀

N.D

GRAVY

-1.6000^c

Hydrophilic residue ratio

40%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Animal
Organism/Source	Bovine
Precursor protein	Hemoglobin β-chain
Residue position	f(34-38)
Precursor protein(s) search	Source.1: DFBPPR16275 ---- Animal proteins ---- Hemoglobin subunit beta Source.2: DFBPPR16779 ---- Animal proteins ---- Hemoglobin subunit beta Source.3: DFBPPR16819 ---- Animal proteins ---- Hemoglobin subunit beta Source.4: DFBPPR18509 ---- Animal proteins ---- Hemoglobin fetal subunit beta Source.5: DFBPPR19968 ---- Animal proteins ---- Hemoglobin subunit epsilon-4 Source.6: DFBPPR8940 ---- Animal proteins ---- Hemoglobin subunit beta Source.7: DFBPPR9275 ---- Animal proteins ---- Hemoglobin subunit epsilon Source.8: DFBPPR9704 ---- Animal proteins ---- Hemoglobin subunit theta Source.9: DFBPPR10352 ---- Animal proteins ---- Hemoglobin subunit beta Source.10: DFBPPR10757 ---- Animal proteins ---- Hemoglobin subunit epsilon Source.11: DFBPPR10957 ---- Animal proteins ---- Hemoglobin subunit rho Source.12: DFBPPR12445 ---- Animal proteins ---- Hemoglobin subunit beta-1/2 Source.13: DFBPPR12812 ---- Animal proteins ---- Hemoglobin subunit gamma Source.14: DFBPPR12916 ---- Animal proteins ---- Hemoglobin subunit epsilon Source.15: DFBPPR13247 ---- Animal proteins ---- Hemoglobin subunit beta Source.16: DFBPPR13439 ---- Animal proteins ---- Hemoglobin subunit beta-A Source.17: DFBPPR13453 ---- Animal proteins ---- Hemoglobin subunit beta-C Source.18: DFBPPR13465 ---- Animal proteins ---- Hemoglobin fetal subunit beta Source.19: DFBPPR13470 ---- Animal proteins ---- Hemoglobin subunit epsilon-2 Source.20: DFBPPR13474 ---- Animal proteins ---- Hemoglobin subunit epsilon-1 Source.21: DFBPPR13618 ---- Animal proteins ---- Hemoglobin subunit beta Source.22: DFBPPR13695 ---- Animal proteins ---- Hemoglobin subunit beta-C Source.23: DFBPPR13859 ---- Animal proteins ---- Hemoglobin fetal subunit beta Source.24: DFBPPR13989 ---- Animal proteins ---- Hemoglobin subunit beta-A/B Source.25: DFBPPR14589 ---- Marine protein ---- Hemoglobin subunit beta-1 Source.26: DFBPPR14865 ---- Marine protein ---- Hemoglobin cathodic subunit beta
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

Peptide H5 exhibited less than 15% inhibition of Dipeptidyl-peptidase IV (EC 3.4.14.5) at 2 mUI at 30 μM, as shown in Figure 1.

Fig. 1. Comparative inhibition effects of seven hemorphins on DPPIV activity. DPPIV enzyme activity was measured at 37 °C in the presence of 0.15 mM of Gly-Pro-pNA, hemorphins concentration of 30 μM and 2 mUI of DPP IV. Inhibition (%) was expressed relative to the control value without inhibitory peptides. Data were the means ± S.D. of three different experiments.

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])(CC(=CN2)C1=C2C=CC=C1)C(=O)N[C@@]([H])([C@]([H])(O)C)C(=O)N[C@@]([H])(CCC(=O)N)C(=O)O

Preparation method

Mode of preparation	Synthesis
Enzyme(s)/starter culture	Hemorphins (LVVH7, VVH7, H7, VVH6, VVH5, H5 and H4) were synthesized by Altergen (Illkirch, France).

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]	DFBPOPIO0059
[D2]	DFBPMUFU0736

[D3]

[D4]

[D5]

[D6]

Reference(s)

Primary literature	Cohen M, Fruitier-Arnaudin I, Piot JM. Hemorphins: substrates and/or inhibitors of dipeptidyl peptidase IV. Hemorphins N-terminus sequence influence on the interaction between hemorphins and DPPIV. Biochimie. 2004 Jan;86(1):31-7. PMID: 14987798 DOI: 10.1016/j.biochi.2003.11.001
Other literature(s)	N.D
PubDate	2004