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 - DFBPACEI0451(ACE-inhibitory peptide)

DFBP ID	DFBPACEI0451
Peptide sequence	YALPHA
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

Tyr-Ala-Leu-Pro-His-Ala

Single-letter amino acid

YALPHA

Peptide length

Peptide mass

Experimental mass	Theoretical mass
N.D	670.75 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

7.74 ^c

IC₅₀

9.8 uM

pIC₅₀

-0.991

GRAVY

0.2167^c

Hydrophilic residue ratio

66.67%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Animal, Marine, Fish
Organism/Source	Squid and mantle, Shiokara
Precursor protein	Squid liver and mantle muscle homogenates
Residue position	N.D
Precursor protein(s) search	Source.1: DFBPPR2763 ---- Plant proteins ---- Actin-1 Source.2: DFBPPR2989 ---- Plant proteins ---- Actin-2 Source.3: DFBPPR3087 ---- Plant proteins ---- Actin-3 Source.4: DFBPPR5185 ---- Plant proteins ---- Actin-1 Source.5: DFBPPR6550 ---- Plant proteins ---- Actin-3 Source.6: DFBPPR6551 ---- Plant proteins ---- Actin-2 Source.7: DFBPPR6552 ---- Plant proteins ---- Actin-1 Source.8: DFBPPR16188 ---- Animal proteins ---- Actin, cytoplasmic 1 Source.9: DFBPPR16883 ---- Animal proteins ---- Actin, aortic smooth muscle Source.10: DFBPPR17154 ---- Animal proteins ---- Actin, cytoplasmic 2 Source.11: DFBPPR17155 ---- Animal proteins ---- Actin, cytoplasmic 2 Source.12: DFBPPR17514 ---- Animal proteins ---- Actin, alpha skeletal muscle Source.13: DFBPPR17747 ---- Animal proteins ---- Actin, cytoplasmic 1 Source.14: DFBPPR18495 ---- Animal proteins ---- Actin, gamma-enteric smooth muscle Source.15: DFBPPR8884 ---- Animal proteins ---- Actin, cytoplasmic 1 Source.16: DFBPPR10103 ---- Animal proteins ---- Actin, cytoplasmic 1 Source.17: DFBPPR10319 ---- Animal proteins ---- Actin, alpha cardiac muscle 1 Source.18: DFBPPR10338 ---- Animal proteins ---- Actin, alpha skeletal muscle Source.19: DFBPPR10431 ---- Animal proteins ---- Actin, aortic smooth muscle Source.20: DFBPPR10478 ---- Animal proteins ---- Actin, gamma-enteric smooth muscle Source.21: DFBPPR10777 ---- Animal proteins ---- Actin, cytoplasmic type 5 Source.22: DFBPPR10810 ---- Animal proteins ---- Actin, cytoplasmic 2 Source.23: DFBPPR12268 ---- Animal proteins ---- Actin, alpha skeletal muscle Source.24: DFBPPR12556 ---- Animal proteins ---- Actin, aortic smooth muscle Source.25: DFBPPR12700 ---- Animal proteins ---- Actin, cytoplasmic 1 Source.26: DFBPPR12701 ---- Animal proteins ---- Actin, cytoplasmic 1 Source.27: DFBPPR13231 ---- Animal proteins ---- Actin, cytoplasmic 1 Source.28: DFBPPR13769 ---- Animal proteins ---- Actin, cytoplasmic 1 Source.29: DFBPPR13996 ---- Animal proteins ---- Actin, alpha skeletal muscle Source.30: DFBPPR14021 ---- Animal proteins ---- Actin, cytoplasmic 1 Source.31: DFBPPR14143 ---- Marine protein ---- Actin, cytoplasmic 1 Source.32: 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 strong Angiotensin-Converting Enzyme (ACE) (EC 3.4.15.1) inhibitory activity with an IC₅₀ value of 9.8 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])(Cc1ccc(O)cc1)C(=O)N[C@@]([H])(C)C(=O)N[C@@]([H])(CC(C)C)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(CC1=CN=C-N1)C(=O)N[C@@]([H])(C)C(=O)O

Preparation method

Mode of preparation	Autolysis
Enzyme(s)/starter culture	The peptide was isolated from the autolysis of squid liver and mantle muscle homogenates.

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

N.D

Database cross-references

[D1]

[D2]

[D3]

[D4]

Reference(s)

Primary literature	Wako Y, Ishikawa S, Muramoto K. Angiotensin I-converting enzyme inhibitors in autolysates of squid liver and mantle muscle. Biosci Biotechnol Biochem. 1996 Aug;60(8):1353-5. PMID: 8987556 DOI: 10.1271/bbb.60.1353
Other literature(s)	N.D
PubDate	1996