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 - DFBPACEI1009(ACE-inhibitory peptide)

DFBP ID	DFBPACEI1009
Peptide sequence	FQPSF
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

Phe-Gln-Pro-Ser-Phe

Single-letter amino acid

FQPSF

Peptide length

Peptide mass

Experimental mass	Theoretical mass
N.D	624.69 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

5.97 ^c

IC₅₀

12.56 uM

pIC₅₀

-1.099

GRAVY

-0.0600^c

Hydrophilic residue ratio

60%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Animal, Marine, Fish
Organism/Source	Skate (Rajiformes: Rajidae)
Precursor protein	Thornback ray muscle (Raja clavata)
Residue position	N.D
Precursor protein(s) search	Source.1: DFBPPR2751 ---- Plant proteins ---- Actin-7 Source.2: DFBPPR2763 ---- Plant proteins ---- Actin-1 Source.3: DFBPPR4726 ---- Plant proteins ---- 40S ribosomal protein S10-2 Source.4: DFBPPR4815 ---- Plant proteins ---- 40S ribosomal protein S10-1 Source.5: DFBPPR16188 ---- Animal proteins ---- Actin, cytoplasmic 1 Source.6: DFBPPR16883 ---- Animal proteins ---- Actin, aortic smooth muscle Source.7: DFBPPR17154 ---- Animal proteins ---- Actin, cytoplasmic 2 Source.8: DFBPPR17155 ---- Animal proteins ---- Actin, cytoplasmic 2 Source.9: DFBPPR17514 ---- Animal proteins ---- Actin, alpha skeletal muscle Source.10: DFBPPR17747 ---- Animal proteins ---- Actin, cytoplasmic 1 Source.11: DFBPPR18495 ---- Animal proteins ---- Actin, gamma-enteric smooth muscle Source.12: DFBPPR8884 ---- Animal proteins ---- Actin, cytoplasmic 1 Source.13: DFBPPR10103 ---- Animal proteins ---- Actin, cytoplasmic 1 Source.14: DFBPPR10319 ---- Animal proteins ---- Actin, alpha cardiac muscle 1 Source.15: DFBPPR10338 ---- Animal proteins ---- Actin, alpha skeletal muscle Source.16: DFBPPR10431 ---- Animal proteins ---- Actin, aortic smooth muscle Source.17: DFBPPR10478 ---- Animal proteins ---- Actin, gamma-enteric smooth muscle Source.18: DFBPPR10777 ---- Animal proteins ---- Actin, cytoplasmic type 5 Source.19: DFBPPR10810 ---- Animal proteins ---- Actin, cytoplasmic 2 Source.20: DFBPPR12268 ---- Animal proteins ---- Actin, alpha skeletal muscle Source.21: DFBPPR12556 ---- Animal proteins ---- Actin, aortic smooth muscle Source.22: DFBPPR12700 ---- Animal proteins ---- Actin, cytoplasmic 1 Source.23: DFBPPR12701 ---- Animal proteins ---- Actin, cytoplasmic 1 Source.24: DFBPPR13231 ---- Animal proteins ---- Actin, cytoplasmic 1 Source.25: DFBPPR13769 ---- Animal proteins ---- Actin, cytoplasmic 1 Source.26: DFBPPR13996 ---- Animal proteins ---- Actin, alpha skeletal muscle Source.27: DFBPPR14021 ---- Animal proteins ---- Actin, cytoplasmic 1 Source.28: DFBPPR14143 ---- Marine protein ---- Actin, cytoplasmic 1 Source.29: 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 12.56 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])(Cc1ccccc1)C(=O)N[C@@]([H])(CCC(=O)N)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(CO)C(=O)N[C@@]([H])(Cc1ccccc1)C(=O)O

Preparation method

Mode of preparation	Enzymatic hydrolysis
Enzyme(s)/starter culture	Thornback ray (Raja clavata) muscle was hydrolyzed with Bacillus subtilis A26 proteases until a hydrolysis degree of 18.35%.

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

BIOPEP-UWM

[D1]

9006, 9174, 9279

APD

[D2]

BioPepDB

[D3]

MBPDB

[D4]

Reference(s)

Primary literature	Lassoued, I., Mora, L., Barkia, A., Aristoy, M.C., Nasri, M., Toldrá, F. Angiotensin I-converting enzyme inhibitory peptides FQPSF and LKYPI identified in Bacillus subtilis A26 hydrolysate of thornback ray muscle. International Journal of Food Science & Technology. 2016, 51, 1604-9. DOI: 10.1111/ijfs.13130
Other literature(s)	N.D
PubDate	2016