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 - DFBPACEI1154(ACE-inhibitory peptide)

DFBP ID	DFBPACEI1154
Peptide sequence	LLYQEPVLGPVRGPFPIIV
Type	Native peptide
Peptide/Function name	ACE-inhibitory peptide

Function-activity relationship

Main bioactivity	ACE-inhibitory activity
Otheir bioactivity	Antihypertensive activity ^[D1], Immunomodulatory activity ^[D2], Multifunctional activity ^[D3]

Calculated physicochemical properties

Three-letter amino acid

Leu-Leu-Tyr-Gln-Glu-Pro-Val-Leu-Gly-Pro-Val-Arg-Gly-Pro-Phe-Pro-Ile-Ile-Val

Single-letter amino acid

LLYQEPVLGPVRGPFPIIV

Peptide length

Peptide mass

Experimental mass	Theoretical mass
N.D	2107.55 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

6.88 ^c

IC₅₀

21 uM

pIC₅₀

-1.322

GRAVY

0.8316^c

Hydrophilic residue ratio

78.95%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Animal
Organism/Source	Milk protein
Precursor protein	β-Casein
Residue position	f(191-209) ^[1]
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 21 μM.
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])(CC(C)C)C(=O)N[C@@]([H])(CC(C)C)C(=O)N[C@@]([H])(Cc1ccc(O)cc1)C(=O)N[C@@]([H])(CCC(=O)N)C(=O)N[C@@]([H])(CCC(=O)O)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(C(C)C)C(=O)N[C@@]([H])(CC(C)C)C(=O)NCC(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(C(C)C)C(=O)N[C@@]([H])(CCCNC(=N)N)C(=O)NCC(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(Cc1ccccc1)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])([C@]([H])(CC)C)C(=O)N[C@@]([H])([C@]([H])(CC)C)C(=O)N[C@@]([H])(C(C)C)C(=O)O

Preparation method

Mode of preparation	Enzymatic hydrolysis.
Enzyme(s)/starter culture	Hydrolysis with an extracellular proteinase from Lactobacillus helveticus CP790.

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

DFBP

[D1]	DFBPANHY0122
[D2]	DFBPIMMU0090
[D3]	DFBPMUFU0227

[D4]

[D5]

[D6]

[D7]

Reference(s)

Primary literature	Yamamoto, N., Akino, A., Takano, T. Antihypertensive Effect of the Peptides Derived from Casein by an Extracellular Proteinase from Lactobacillus helveticus CP790. Journal of Dairy Science. 1994, 77, 917-22. DOI: 10.3168/jds.S0022-0302(94)77026-0
Other literature(s)	[1] Ha, G.E., et al., Identification of Antihypertensive Peptides Derived from Low Molecular Weight Casein Hydrolysates Generated during Fermentation by Bifidobacterium longum KACC 91563. Korean Journal for Food Science of Animal Resources, 2015. 35(6): p. 738-747.
PubDate	1994