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 - DFBPACEI0106(ACE-inhibitory peptide)

DFBP ID	DFBPACEI0106
Peptide sequence	VVYPWTQRF
Type	Native peptide
Peptide/Function name	ACE-inhibitory peptide, VV-hemorphin-7 ^[1]

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	1195.39 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

9.82 ^c

IC₅₀

66 umol/L

pIC₅₀

-1.82

GRAVY

-0.1444^c

Hydrophilic residue ratio

55.56%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Marine
Organism/Source	Oyster (Crassostrea talienwhanensis Crosse)
Precursor protein	Oyster protein hydrolysate
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: DFBPACEI1004----Bovine blood----Bovine hemoglobin

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 66 umol/L, 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	Oyster protein solution was digested with pepsin at a protein substrate to enzyme ratio of 100:1.5 (w/w) at pH 2.0 and a temperature of 37 ℃ for 24 h.

Stability & Cytotoxicity

Peptide stability

Literature report:	Stability study for ACE inhibitory activity showed that the isolated nonapeptide had the good heat and pH stability and strong enzyme-resistant properties against gastrointestinal proteases.
EHP-Tool:	Enzymatic Hydrolysis Prediction Tool (EHP-Tool)

Peptide cytotoxicity

Literature report:	N.D
Prediction:	ToxinPred

Additional information

Oyster is an abundant resource from Oceans and pepsin treatment for oyster proteins is an effective cheap means of production contrasting with synthesis of pure peptide.

Database cross-references

DFBP

[D1]	DFBPANHY0598
[D2]	DFBPDPIV0227
[D3]	DFBPOPIO0016
[D4]	DFBPMUFU0043

[D5]

[D6]

[D7]

[D8]

Reference(s)

Primary literature	Wang J, Hu J, Cui J, Bai X, Du Y, Miyaguchi Y, Lin B. Purification and identification of a ACE inhibitory peptide from oyster proteins hydrolysate and the antihypertensive effect of hydrolysate in spontaneously hypertensive rats. Food Chem. 2008 Nov 15;111(2):302-8. PMID: 26047427 DOI: 10.1016/j.foodchem.2008.03.059
Other literature(s)	[1] Zhao Q, Sannier F, Garreau I, et al. Inhibition and inhibition kinetics of angiotensin converting enzyme activity by hemorphins, isolated from a peptic bovine hemoglobin hydrolysate[J]. Biochemical & Biophysical Research Communications, 1994, 204(1):216. [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	2008