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 - DFBPACEI0235(ACE-inhibitory peptide)

DFBP ID	DFBPACEI0235
Peptide sequence	EKSYELP
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

Glu-Lys-Ser-Tyr-Glu-Leu-Pro

Single-letter amino acid

EKSYELP

Peptide length

Peptide mass

Experimental mass	Theoretical mass
865.1 Da	864.94 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

4.33 ^c

IC₅₀

14.41 uM

pIC₅₀

-1.159

GRAVY

-1.5429^c

Hydrophilic residue ratio

28.57%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Animal, Fish, Marine
Organism/Source	Cuttlefish (Sepia officinalis)
Precursor protein	Muscle protein hydrolysates
Residue position	N.D
Precursor protein(s) search	Source.1: DFBPPR2751 ---- Plant proteins ---- Actin-7 Source.2: DFBPPR2763 ---- Plant proteins ---- Actin-1 Source.3: DFBPPR2989 ---- Plant proteins ---- Actin-2 Source.4: DFBPPR3087 ---- Plant proteins ---- Actin-3 Source.5: DFBPPR5185 ---- Plant proteins ---- Actin-1 Source.6: DFBPPR16188 ---- Animal proteins ---- Actin, cytoplasmic 1 Source.7: DFBPPR16883 ---- Animal proteins ---- Actin, aortic smooth muscle Source.8: DFBPPR17154 ---- Animal proteins ---- Actin, cytoplasmic 2 Source.9: DFBPPR17155 ---- Animal proteins ---- Actin, cytoplasmic 2 Source.10: DFBPPR17514 ---- Animal proteins ---- Actin, alpha skeletal muscle Source.11: DFBPPR17747 ---- Animal proteins ---- Actin, cytoplasmic 1 Source.12: DFBPPR18495 ---- Animal proteins ---- Actin, gamma-enteric smooth muscle Source.13: DFBPPR8884 ---- Animal proteins ---- Actin, cytoplasmic 1 Source.14: DFBPPR10103 ---- Animal proteins ---- Actin, cytoplasmic 1 Source.15: DFBPPR10319 ---- Animal proteins ---- Actin, alpha cardiac muscle 1 Source.16: DFBPPR10338 ---- Animal proteins ---- Actin, alpha skeletal muscle Source.17: DFBPPR10431 ---- Animal proteins ---- Actin, aortic smooth muscle Source.18: DFBPPR10478 ---- Animal proteins ---- Actin, gamma-enteric smooth muscle Source.19: DFBPPR10777 ---- Animal proteins ---- Actin, cytoplasmic type 5 Source.20: DFBPPR10810 ---- Animal proteins ---- Actin, cytoplasmic 2 Source.21: DFBPPR12268 ---- Animal proteins ---- Actin, alpha skeletal muscle Source.22: DFBPPR12556 ---- Animal proteins ---- Actin, aortic smooth muscle Source.23: DFBPPR12700 ---- Animal proteins ---- Actin, cytoplasmic 1 Source.24: DFBPPR12701 ---- Animal proteins ---- Actin, cytoplasmic 1 Source.25: DFBPPR13231 ---- Animal proteins ---- Actin, cytoplasmic 1 Source.26: DFBPPR13769 ---- Animal proteins ---- Actin, cytoplasmic 1 Source.27: DFBPPR13996 ---- Animal proteins ---- Actin, alpha skeletal muscle Source.28: DFBPPR14021 ---- Animal proteins ---- Actin, cytoplasmic 1 Source.29: DFBPPR14143 ---- Marine protein ---- Actin, cytoplasmic 1 Source.30: DFBPPR14935 ---- Microorganism protein ---- Actin Source.31: DFBPPR7844 ---- Plant protein ---- Actin-1
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 potent Angiotensin-Converting Enzyme (ACE) (EC 3.4.15.1) inhibitory activity with an IC₅₀ value of 14.41 uM.
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])(CCC(=O)O)C(=O)N[C@@]([H])(CCCCN)C(=O)N[C@@]([H])(CO)C(=O)N[C@@]([H])(Cc1ccc(O)cc1)C(=O)N[C@@]([H])(CCC(=O)O)C(=O)N[C@@]([H])(CC(C)C)C(=O)N1[C@@]([H])(CCC1)C(=O)O

Preparation method

Mode of preparation	Enzymatic hydrolysis
Enzyme(s)/starter culture	Hydrolysis with crude enzyme from B. mojavensis A21 and cuttlefish hepatopancreas.

Stability & Cytotoxicity

Peptide stability

Literature report:	N.D
EHP-Tool:	Enzymatic Hydrolysis Prediction Tool (EHP-Tool)

Peptide cytotoxicity

Literature report:	N.D
Prediction:	ToxinPred

Additional information

The ACE inhibitory peptide from cuttlefish muscle protein hydrolysates could be potential candidates for the development of nutraceuticals and pharmaceuticals active against hypertension and its related diseases.

Database cross-references

[D1]

[D2]

[D3]

[D4]

Reference(s)

Primary literature	Balti R, Bougatef A, Sila A, Guillochon D, Dhulster P, Nedjar-Arroume N. Nine novel angiotensin I-converting enzyme (ACE) inhibitory peptides from cuttlefish (Sepia officinalis) muscle protein hydrolysates and antihypertensive effect of the potent active peptide in spontaneously hypertensive rats. Food Chem. 2015 Mar 1;170:519-25. PMID: 25306378 DOI: 10.1016/j.foodchem.2013.03.091
Other literature(s)	[1] Nakamura Y, Yamamoto N, Sakai K, et al. Purification and Characterization of Angiotensin I-Converting Enzyme Inhibitors from Sour Milk[J]. Journal of Dairy Science, 1995, 78(4):777-783.
PubDate	2015