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 - DFBPACEI0427(ACE-inhibitory peptide)

DFBP ID	DFBPACEI0427
Peptide sequence	YQEPVLGPVRGPFPIIV
Type	Native peptide
Peptide/Function name	ACE-inhibitory peptide

Function-activity relationship

Main bioactivity	ACE-inhibitory activity
Otheir bioactivity	Antihypertensive activity ^[D1], Antimicrobial activity ^[D2], Antithrombotic activity ^[D3], Immunomodulatory activity ^[D4], Multifunctional activity ^[D5]

Calculated physicochemical properties

Three-letter amino acid

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

Single-letter amino acid

YQEPVLGPVRGPFPIIV

Peptide length

Peptide mass

Experimental mass	Theoretical mass
1881.091 Da ^[2]	1881.24 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

6.88 ^c

IC₅₀

101 uM

pIC₅₀

-2.004

GRAVY

0.4824^c

Hydrophilic residue ratio

76.47%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Animal
Organism/Source	Bovine milk
Precursor protein	β-Casein
Residue position	N.D
Precursor protein(s) search	Source.1: DFBPPR7718 ---- Milk proteins ---- Beta-casein Source.2: DFBPPR8489 ---- Milk proteins ---- Beta-casein
Link-research Inductive analysis	Link 1: DFBPACEI1401----Bovine milk protein----β-Casein

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 101 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])(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

The results of the present work provide a basis for further applications of M. pomifera proteases in the food industry for the development of functional foods and nutraceuticals ^[2].

Database cross-references

DFBP

[D1]	DFBPANHY0117
[D2]	DFBPAMIC0198
[D3]	DFBPANTH0103
[D4]	DFBPIMMU0033
[D5]	DFBPMUFU0119

[D6]

[D7]

[D8]

[D9]

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] Coste M, Rochet V, Léonil J, et al. Identification of C-terminal peptides of bovine beta-casein that enhance proliferation of rat lymphocytes.[J]. Immunology Letters, 1992, 33(1):41-6. [2] Corrons, María Alicia, Liggieri C S , Trejo, Sebastián Alejandro, et al. ACE-inhibitory peptides from bovine caseins released with peptidases from Maclura pomifera latex[J]. Food Research International, 2017, 93:8-15.
PubDate	1994