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 - DFBPACEI1775(ACE-inhibitory peptide)

DFBP ID	DFBPACEI1775
Peptide sequence	LVVYPWTQRF
Type	Native peptide
Peptide/Function name	ACE-inhibitory peptide, LVV-hemorphin-7, LVV-h7

Function-activity relationship

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

1.7 μM

pIC₅₀

-0.23

GRAVY

0.2500^c

Hydrophilic residue ratio

60%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Animal
Organism/Source	Bovine blood
Precursor protein	Bovine hemoglobin
Residue position	N.D
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

ACE-inhibitory activity	The peptide exhibited strong Angiotensin-Converting Enzyme (ACE) (EC 3.4.15.1) inhibitory activity with an IC₅₀ value of 1.7 uM, and its ACE inhibitory pattern was shown by Lineweaver–Burk plots to be a non-competitive inhibition pattern.
Specific target protein(s)	Specific Target Protein(s): Angiotensin-converting enzyme

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	Bovine hemoglobin hydrolysate was obtained at pilot-scale by peptic hydrolysis in an ultrafiltration reactor.

Stability & Cytotoxicity

Peptide stability

Literature report:	When LVV-hemorphin-7 was incubated with ACE the Arg-Phe bond was cleaved and gave no further cleavage of LVV-hemorphin-5.
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 ^[1].

Database cross-references

DFBP

[D1]	DFBPDPIV0221
[D2]	DFBPOPIO0136
[D3]	DFBPMUFU0520

[D4]

[D5]

[D6]

[D7]

Reference(s)

Primary literature	Zhao Q, Sannier F, Garreau I, Guillochon D, Piot JM. Inhibition and inhibition kinetics of angiotensin converting enzyme activity by hemorphins, isolated from a peptic bovine hemoglobin hydrolysate. Biochem Biophys Res Commun. 1994 Oct 14;204(1):216-23. PMID: 7945362 DOI: 10.1006/bbrc.1994.2447
Other literature(s)	[1] 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	1994