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 - DFBPACEI1004(ACE-inhibitory peptide)

DFBP ID	DFBPACEI1004
Peptide sequence	VVYPWTQRF
Type	Native peptide
Peptide/Function name	ACE-inhibitory peptide, VV-hemorphin-7

Function-activity relationship

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

Calculated physicochemical properties

Three-letter amino acid

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

Single-letter amino acid

VVYPWTQRF

Peptide length

Peptide mass

Experimental mass	Theoretical mass
1195 Da ^[1]	1195.39 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

9.82 ^c

IC₅₀

10.2 uM

pIC₅₀

-1.009

GRAVY

-0.1444^c

Hydrophilic residue ratio

55.56%^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	Link 1: DFBPACEI0106----Oyster (Crassostrea talienwhanensis Crosse)----Oyster protein hydrolysate

Biological/Functional activity & target protein

ACE-inhibitory activity	The peptide exhibited potent Angiotensin-Converting Enzyme (ACE) (EC 3.4.15.1) inhibitory activity with an IC₅₀ value of 10.2 uM (66 umol/L ^[1]), 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	Bitter peptide according to the BIOPEP database of sensory peptides and amino acids (ID 404).
Bitter prediction tools	Bitter taste ^prediction

SMILES

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 VV-hemorphin-7 was incubated with ACE the Gln-Arg bond was cleaved and VV-hemorphin-5 appeared. The later was then relatively stable and remained even after 7 h.
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]	DFBPANHY0598
[D2]	DFBPDPIV0227
[D3]	DFBPOPIO0016
[D4]	DFBPMUFU0043

[D5]

[D6]

[D7]

[D8]

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] Wang J, Hu J, Cui J, et al. Purification and identification of a ACE inhibitory peptide from oyster proteins hydrolysate and the antihypertensive effect of hydrolysate in spontaneously hypertensive rats.[J]. Food Chemistry, 2008, 111(2):302-8. [2] GarreauI, Zhao Q, Pejoan C, et al. VV-hemorphin-7 and LVV-hemorphin-7 released during in vitro peptic hemoglobin hydrolysis are morphinomimetic peptides.[J]. Neuropeptides, 1995, 28(4):243. [3] 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.
PubDate	1994