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 - DFBPACEI0134(ACE-inhibitory peptide)

DFBP ID	DFBPACEI0134
Peptide sequence	VIIF
Type	Native peptide
Peptide/Function name	ACE-inhibitory peptide

Function-activity relationship

Main bioactivity	ACE-inhibitory activity
Otheir bioactivity	N.D

Calculated physicochemical properties

Three-letter amino acid

Val-Ile-Ile-Phe

Single-letter amino acid

VIIF

Peptide length

Peptide mass

Experimental mass	Theoretical mass
491.1 Da	490.63 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

5.97 ^c

IC₅₀

8.7 uM

pIC₅₀

-0.94

GRAVY

4.0000^c

Hydrophilic residue ratio

100%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Marine
Organism/Source	Cuttlefish (Sepia officinalis)
Precursor protein	The muscle of Cuttlefish
Residue position	N.D
Precursor protein(s) search	Source.1: DFBPPR0955 ---- Plant proteins ---- Gibberellin receptor GID1 Source.2: DFBPPR1830 ---- Plant proteins ---- Endoribonuclease Dicer homolog 3a Source.3: DFBPPR1990 ---- Plant proteins ---- DEAD-box ATP-dependent RNA helicase 38 Source.4: DFBPPR2073 ---- Plant proteins ---- ABC transporter G family member 43 Source.5: DFBPPR2074 ---- Plant proteins ---- Potassium transporter 7 Source.6: DFBPPR2539 ---- Plant proteins ---- Probable aldehyde oxidase 1 Source.7: DFBPPR2793 ---- Plant proteins ---- MADS-box transcription factor 33 Source.8: DFBPPR2987 ---- Plant proteins ---- 1-Cys peroxiredoxin B Source.9: DFBPPR3376 ---- Plant proteins ---- DEAD-box ATP-dependent RNA helicase 28 Source.10: DFBPPR3982 ---- Plant proteins ---- DEAD-box ATP-dependent RNA helicase 25 Source.11: DFBPPR4029 ---- Plant proteins ---- Putative multidrug resistance protein Source.12: DFBPPR4427 ---- Plant proteins ---- Probable auxin efflux carrier component 9 Source.13: DFBPPR4534 ---- Plant proteins ---- Protein argonaute 4A Source.14: DFBPPR4868 ---- Plant proteins ---- Putative B3 domain-containing protein Os08g0325100 Source.15: DFBPPR4869 ---- Plant proteins ---- Putative B3 domain-containing protein LOC_Os07g12820 Source.16: DFBPPR6225 ---- Plant proteins ---- 1,4-alpha-glucan-branching enzyme 1, chloroplastic/amyloplastic Source.17: DFBPPR16436 ---- Animal proteins ---- Glycogen debranching enzyme Source.18: DFBPPR16975 ---- Animal proteins ---- Glycerophosphocholine choline phosphodiesterase ENPP6 Source.19: DFBPPR17057 ---- Animal proteins ---- Cation-independent mannose-6-phosphate receptor Source.20: DFBPPR18588 ---- Animal proteins ---- CD166 antigen Source.21: DFBPPR19033 ---- Animal proteins ---- Collagen alpha-2(XI) chain Source.22: DFBPPR20550 ---- Animal proteins ---- G-protein coupled receptor family C group 6 member A Source.23: DFBPPR22589 ---- Animal proteins ---- Transmembrane protein 171 Source.24: DFBPPR8558 ---- Animal proteins ---- Glycerophosphocholine cholinephosphodiesterase ENPP6 Source.25: DFBPPR8717 ---- Animal proteins ---- Rhodopsin Source.26: DFBPPR9496 ---- Animal proteins ---- C-X-C motif chemokine 16 Source.27: DFBPPR10641 ---- Animal proteins ---- Signal peptide peptidase-like 2B Source.28: DFBPPR10857 ---- Animal proteins ---- Smoothened homolog Source.29: DFBPPR10905 ---- Animal proteins ---- Probable G-protein coupled receptor 149 Source.30: DFBPPR12555 ---- Animal proteins ---- Glycogen debranching enzyme Source.31: DFBPPR13151 ---- Animal proteins ---- Transferrin receptor protein 1 Source.32: DFBPPR13190 ---- Animal proteins ---- Sodium channel protein type 4 subunit alpha Source.33: DFBPPR13268 ---- Animal proteins ---- Glycogen debranching enzyme Source.34: DFBPPR13551 ---- Animal proteins ---- Cytochrome P450 1A1 Source.35: DFBPPR14040 ---- Animal proteins ---- NADH-ubiquinone oxidoreductase chain 1 Source.36: DFBPPR14159 ---- Marine protein ---- NADH-ubiquinone oxidoreductase chain 1 Source.37: DFBPPR15008 ---- Microorganism protein ---- ATP-dependent RNA helicase ROK1 Source.38: DFBPPR15011 ---- Microorganism protein ---- Cytochrome b Source.39: DFBPPR15039 ---- Microorganism protein ---- ATP-dependent RNA helicase SUB2 Source.40: DFBPPR15162 ---- Microorganism protein ---- MFS-type transporter PUL3 Source.41: DFBPPR15319 ---- Microorganism protein ---- Glucose transport transcription regulator RGT1 Source.42: DFBPPR15564 ---- Microorganism protein ---- Protein ZIP2
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 8.7 μM, 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])(C(C)C)C(=O)N[C@@]([H])([C@]([H])(CC)C)C(=O)N[C@@]([H])([C@]([H])(CC)C)C(=O)N[C@@]([H])(Cc1ccccc1)C(=O)O

Preparation method

Mode of preparation	Enzymatic hydrolysis
Enzyme(s)/starter culture	Hydrolysis with various digestive proteases obtained by treatment with crude enzyme from cuttlefish hepatopancreas.

Stability & Cytotoxicity

Peptide stability

Literature report:

(1) No apparent change was observed after in vitro incubation with gastrointestinal proteases (including pepsin, trypsin and chymotrypsin, p > 0.05), suggesting that peptides may be resistant to digestion in the gastrointestinal tract, and that the active sequence of the peptide would not be destroyed by these proteases. In addition, peptides were found to be stable after incubation simultaneously with the digestive enzymes.
(2) The heat-stability results showed that preincubation did not change the inhibitory activity of the purified peptides and IC₅₀ values of peptides before and after preincubation were the same (data not shown).

EHP-Tool:

Enzymatic Hydrolysis Prediction Tool (EHP-Tool)

Peptide cytotoxicity

Literature report:	N.D
Prediction:	ToxinPred

Additional information

(1) The stability study results indicate that these peptides may have a potential antihypertensive effect.
(2) Some peptides from cuttlefish could be a beneficial ingredient for nutraceuticals against hypertension.

Database cross-references

[D1]

[D2]

[D3]

[D4]

Reference(s)

Primary literature	Balti, R., Nedjar-Arroume, N., Bougatef, A., Guillochon, D., Nasri, M. Three novel angiotensin I-converting enzyme (ACE) inhibitory peptides from cuttlefish (Sepia officinalis) using digestive proteases. Food Research International. 2010, 43, 1136-43. DOI: 10.1016/j.foodres.2010.02.013
Other literature(s)	N.D
PubDate	2010