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 - DFBPACEI0439(ACE-inhibitory peptide)

DFBP ID	DFBPACEI0439
Peptide sequence	FAQTQSLVYP
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-Ala-Gln-Thr-Gln-Ser-Leu-Val-Tyr-Pro

Single-letter amino acid

FAQTQSLVYP

Peptide length

Peptide mass

Experimental mass	Theoretical mass
N.D	1153.29 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

5.92 ^c

IC₅₀

25 μM

pIC₅₀

-1.398

GRAVY

0.1200^c

Hydrophilic residue ratio

50%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Animal
Organism/Source	Milk protein (Bovine, Buffalo, Ovine)
Precursor protein	β-Casein
Residue position	f(52-61)
Precursor protein(s) search	Source.1: DFBPPR7718 ---- Milk proteins ---- Beta-casein Source.2: DFBPPR8489 ---- Milk proteins ---- Beta-casein
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 25 uM.
Specific target protein(s)	Specific Target Protein(s): Angiotensin-converting enzyme

Taste properties & Structure

Bitterness

Literature report	N.D
Bitter prediction tools	No prediction can be made about the peptide bitterness. ^prediction

SMILES

N[C@@]([H])(Cc1ccccc1)C(=O)N[C@@]([H])(C)C(=O)N[C@@]([H])(CCC(=O)N)C(=O)N[C@@]([H])([C@]([H])(O)C)C(=O)N[C@@]([H])(CCC(=O)N)C(=O)N[C@@]([H])(CO)C(=O)N[C@@]([H])(CC(C)C)C(=O)N[C@@]([H])(C(C)C)C(=O)N[C@@]([H])(Cc1ccc(O)cc1)C(=O)N1[C@@]([H])(CCC1)C(=O)O

Preparation method

Mode of preparation	Synthesis
Enzyme(s)/starter culture	The peptide synthesis was done by the stepwise solid-phase method, using Fmoc-amino acids and mild acid labile side chain protection.

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	Kohmura, M., Nio, N., Ariyoshi, Y. Inhibition of Angiotensin-Converting Enzyme by Synthetic Peptide Fragments of Variousβ-Caseins. Agricultural and Biological Chemistry. 2014, 54, 1101-2. DOI: 10.1080/00021369.1990.10870065
Other literature(s)	N.D
PubDate	2014