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 - DFBPOPIO0136(Opioid peptide)

DFBP ID	DFBPOPIO0136
Peptide sequence	LVVYPWTQRF
Type	Native peptide
Peptide/Function name	Opioid peptide, LVV-hemorphin-7, LVV-h7

Function-activity relationship

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

Calculated physicochemical properties

Three-letter amino acid

Leu-Val-Val-Tyr-Pro-Trp-Thr-Gln-Arg-Phe

Single-letter amino acid

LVVYPWTQRF

Peptide length

Peptide mass

Experimental mass	Theoretical mass
N.D	1308.54 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

9.82 ^c

IC₅₀

N.D

pIC₅₀

N.D

GRAVY

0.2500^c

Hydrophilic residue ratio

60%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Animal
Organism/Source	Bovine
Precursor protein	Hemoglobin β-chain
Residue position	f(31-40)
Precursor protein(s) search	Source.1: DFBPPR16819 ---- Animal proteins ---- Hemoglobin subunit beta Source.2: DFBPPR18509 ---- Animal proteins ---- Hemoglobin fetal subunit beta Source.3: DFBPPR8940 ---- Animal proteins ---- Hemoglobin subunit beta Source.4: DFBPPR9275 ---- Animal proteins ---- Hemoglobin subunit epsilon Source.5: DFBPPR9704 ---- Animal proteins ---- Hemoglobin subunit theta Source.6: DFBPPR12445 ---- Animal proteins ---- Hemoglobin subunit beta-1/2 Source.7: DFBPPR12812 ---- Animal proteins ---- Hemoglobin subunit gamma Source.8: DFBPPR12916 ---- Animal proteins ---- Hemoglobin subunit epsilon Source.9: DFBPPR13247 ---- Animal proteins ---- Hemoglobin subunit beta Source.10: DFBPPR13439 ---- Animal proteins ---- Hemoglobin subunit beta-A Source.11: DFBPPR13453 ---- Animal proteins ---- Hemoglobin subunit beta-C Source.12: DFBPPR13465 ---- Animal proteins ---- Hemoglobin fetal subunit beta Source.13: DFBPPR13474 ---- Animal proteins ---- Hemoglobin subunit epsilon-1 Source.14: DFBPPR13618 ---- Animal proteins ---- Hemoglobin subunit beta Source.15: DFBPPR13695 ---- Animal proteins ---- Hemoglobin subunit beta-C Source.16: DFBPPR13859 ---- Animal proteins ---- Hemoglobin fetal 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

Opioid activity

Binding experiments strongly confirm that LVV-hemorphin-7 is opioid peptide since it inhibited [³H]naloxone binding to rat brain membranes. The results indicated that it was nearly as potent as hemorphins-4 and -5 and lesspotent than hemorphin-6 and the hemorphin-7. It appears to be μ/δ-receptor.

Table 1 Opioid activity of VV-hemorphin-7, LVV-hemorphin-7 and various hemorphins.
Peptide	Potencies in the GPI IC₅₀-values (uM)	Affinities for binding sites IC₅₀-values (uM)
Peptide	Potencies in the GPI IC₅₀-values (uM)	[³H]naloxone	[³H]DAGO
YPWT	45.2	n.d.	3.46
YPWTQ	46.1	n.d.	n.d.
YPWTQR	4.3	n.d.	2.00
YPWTQRF	2.9	1.78	1.30
VV-hemorphin-7	34.3	15.2	53.8
LVV-hemorphin-7	29.1	30.7	n.d.

Specific target protein(s)

Specific Target Protein(s):
Mu-type opioid receptor
Delta-type opioid receptor

Taste properties & Structure

Bitterness

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

SMILES

N[C@@]([H])(CC(C)C)C(=O)N[C@@]([H])(C(C)C)C(=O)N[C@@]([H])(C(C)C)C(=O)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)N[C@@]([H])(CCCNC(=N)N)C(=O)N[C@@]([H])(Cc1ccccc1)C(=O)O

Preparation method

Mode of preparation	Enzymatic hydrolysis
Enzyme(s)/starter culture	The peptide was generated by in vitro pepsin treatment of bovine hemoglobin.

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

Selective preparation of this peptide is proposed by a microfluidic-based continuous reaction-separation process. Hemoglobin hydrolysis in microreactor was firstly coupled to LVV-h7 LLE in octan-1-ol and then coupled to LVV-h7 back LLE in acidic water. This continuous process allowed to prepare pure LVV-h7, as confirmed by liquid chromatography and mass spectrometry ^[4].

Database cross-references

DFBP

[D1]	DFBPACEI1775
[D2]	DFBPDPIV0221
[D3]	DFBPMUFU0520

[D4]

[D5]

[D6]

[D7]

Reference(s)

Primary literature	Garreau I, Zhao Q, Pejoan C, Cupo A, Piot JM. VV-hemorphin-7 and LVV-hemorphin-7 released during in vitro peptic hemoglobin hydrolysis are morphinomimetic peptides. Neuropeptides. 1995 Apr;28(4):243-50. PMID: 7596489 DOI: 10.1016/0143-4179(95)90028-4
Other literature(s)	[1] Szikra J, Benyhe S, Orosz G, et al. Radioligand Binding Properties of VV-Hemorphin 7, an Atypical Opioid Peptide ☆[J]. Biochem Biophys Res Commun, 2001, 281(3):670-677. [2] Nyberg F, Sanderson K, Glämsta E L. The hemorphins: a new class of opioid peptides derived from the blood protein hemoglobin.[J]. Peptide Science, 1997, 43(2):147-156. [3] Zhao Q, Garreau I, Sannier F, et al. Opioid peptides derived from hemoglobin: Hemorphins[J]. Peptide Science, 1997, 43(2):75-98. [4] Dhulster, Pascal, Froidevaux, et al. Sustainable efficient way for opioid peptide LVV-h7 preparation from enzymatic proteolysis in a microfluidic-based reaction-extraction process with solvent recycling[J]. Journal of Chromatography B Analytical Technologies in the Biomedical & Life Sciences, 2016.
PubDate	1995