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 - DFBPACEI0133(ACE-inhibitory peptide)

DFBP ID	DFBPACEI0133
Peptide sequence	VYAP
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-Tyr-Ala-Pro

Single-letter amino acid

VYAP

Peptide length

Peptide mass

Experimental mass	Theoretical mass
448.2 Da	448.51 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

5.92 ^c

IC₅₀

6.1 uM

pIC₅₀

-0.785

GRAVY

0.7750^c

Hydrophilic residue ratio

75%^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: DFBPPR0813 ---- Plant proteins ---- Protein RICE FLOWERING LOCUS T 1 Source.2: DFBPPR0819 ---- Plant proteins ---- Homeobox-leucine zipper protein ROC1 Source.3: DFBPPR0822 ---- Plant proteins ---- Homeobox-leucine zipper protein ROC4 Source.4: DFBPPR0829 ---- Plant proteins ---- Homeobox-leucine zipper protein ROC5 Source.5: DFBPPR0830 ---- Plant proteins ---- Homeobox-leucine zipper protein ROC6 Source.6: DFBPPR0858 ---- Plant proteins ---- Bidirectional sugar transporter SWEET11 Source.7: DFBPPR1407 ---- Plant proteins ---- Indole-3-acetate O-methyltransferase 1 Source.8: DFBPPR1436 ---- Plant proteins ---- Bidirectional sugar transporter SWEET14 Source.9: DFBPPR1473 ---- Plant proteins ---- Protein HEADING DATE 3A Source.10: DFBPPR1489 ---- Plant proteins ---- Protein SUBSTANDARD STARCH GRAIN 4, chloroplastic Source.11: DFBPPR1663 ---- Plant proteins ---- Cyclin-H1-1 Source.12: DFBPPR1853 ---- Plant proteins ---- Laccase-4 Source.13: DFBPPR2034 ---- Plant proteins ---- Kinesin-like protein KIN-8B Source.14: DFBPPR2346 ---- Plant proteins ---- Probable tocopherol cyclase, chloroplastic Source.15: DFBPPR2426 ---- Plant proteins ---- Transcription factor NIGT1 Source.16: DFBPPR4063 ---- Plant proteins ---- Cleavage and polyadenylation specificity factor subunit 2 Source.17: DFBPPR4933 ---- Plant proteins ---- Cinnamyl alcohol dehydrogenase 7 Source.18: DFBPPR5478 ---- Plant proteins ---- 1,4-alpha-glucan-branching enzyme 2, chloroplastic/amyloplastic Source.19: DFBPPR6225 ---- Plant proteins ---- 1,4-alpha-glucan-branching enzyme 1, chloroplastic/amyloplastic Source.20: DFBPPR6510 ---- Plant proteins ---- 50S ribosomal protein 6, chloroplastic Source.21: DFBPPR16332 ---- Animal proteins ---- Transcription factor 4 Source.22: DFBPPR16333 ---- Animal proteins ---- Transcription factor 4 Source.23: DFBPPR17122 ---- Animal proteins ---- Glycine receptor subunit beta Source.24: DFBPPR17488 ---- Animal proteins ---- Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase 3 Source.25: DFBPPR19306 ---- Animal proteins ---- Splicing factor 3A subunit 1 Source.26: DFBPPR19318 ---- Animal proteins ---- Ubiquinone biosynthesis O-methyltransferase, mitochondrial Source.27: DFBPPR19882 ---- Animal proteins ---- Cytoplasmic tRNA 2-thiolation protein 1 Source.28: DFBPPR20046 ---- Animal proteins ---- Leukocyte cell-derived chemotaxin-2 Source.29: DFBPPR20603 ---- Animal proteins ---- Craniofacial development protein 2 Source.30: DFBPPR20777 ---- Animal proteins ---- Sodium-coupled monocarboxylate transporter 2 Source.31: DFBPPR21527 ---- Animal proteins ---- Programmed cell death protein 2 Source.32: DFBPPR11015 ---- Animal proteins ---- Myeloid protein 1 Source.33: DFBPPR11300 ---- Animal proteins ---- MAM domain-containing glycosylphosphatidylinositol anchor protein 1 Source.34: DFBPPR11334 ---- Animal proteins ---- Heme oxygenase 1 Source.35: DFBPPR12296 ---- Animal proteins ---- Neprilysin Source.36: DFBPPR13674 ---- Animal proteins ---- Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase 3 Source.37: DFBPPR15590 ---- Microorganism protein ---- Protein transport protein SEC9
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 6.1 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])(Cc1ccc(O)cc1)C(=O)N[C@@]([H])(C)C(=O)N1[C@@]([H])(CCC1)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