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 - DFBPACEI1441(ACE-inhibitory peptide)

DFBP ID	DFBPACEI1441
Peptide sequence	NENLLRFFVAPFPEVFG
Type	Native peptide
Peptide/Function name	ACE-inhibitory peptide

Function-activity relationship

Main bioactivity	ACE-inhibitory activity
Otheir bioactivity	Anticancer activity ^[D1], Multifunctional activity ^[D2]

Calculated physicochemical properties

Three-letter amino acid

Asn-Glu-Asn-Leu-Leu-Arg-Phe-Phe-Val-Ala-Pro-Phe-Pro-Glu-Val-Phe-Gly

Single-letter amino acid

NENLLRFFVAPFPEVFG

Peptide length

Peptide mass

Experimental mass	Theoretical mass
N.D	1996.28 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

4.33 ^c

IC₅₀

55 μM

pIC₅₀

-1.74

GRAVY

0.4059^c

Hydrophilic residue ratio

70.59%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Animal
Organism/Source	Milk protein
Precursor protein	α_s1-Casein
Residue position	f(32-48)
Precursor protein(s) search	Source.1: DFBPPR7717 ---- Milk proteins ---- Alpha-S1-casein Source.2: DFBPPR8488 ---- Milk proteins ---- Alpha-S1-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 55 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(=O)N)C(=O)N[C@@]([H])(CCC(=O)O)C(=O)N[C@@]([H])(CC(=O)N)C(=O)N[C@@]([H])(CC(C)C)C(=O)N[C@@]([H])(CC(C)C)C(=O)N[C@@]([H])(CCCNC(=N)N)C(=O)N[C@@]([H])(Cc1ccccc1)C(=O)N[C@@]([H])(Cc1ccccc1)C(=O)N[C@@]([H])(C(C)C)C(=O)N[C@@]([H])(C)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(Cc1ccccc1)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(CCC(=O)O)C(=O)N[C@@]([H])(C(C)C)C(=O)N[C@@]([H])(Cc1ccccc1)C(=O)NCC(=O)O

Preparation method

Mode of preparation	Fermentation
Enzyme(s)/starter culture	Milk proteins was fermented with Lactobacillus (Lb.) helveticus NCC 2765.

Stability & Cytotoxicity

Peptide stability

Literature report:	Pepsin hydrolyzed α_s1-casein-derived peptide (NENLLRFFVAPFPEVFG) between the two phenylalanine residues and corresponding to the fragments NENLLRF and FVAPFPEVFG.
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]	DFBPANCA0090, DFBPANCA0105
[D2]	DFBPMUFU0385

[D3]

[D4]

[D5]

[D6]

Reference(s)

Primary literature	Robert MC, Razaname A, Mutter M, Juillerat MA. Identification of angiotensin-I-converting enzyme inhibitory peptides derived from sodium caseinate hydrolysates produced by Lactobacillus helveticus NCC 2765. J Agric Food Chem. 2004 Nov 17;52(23):6923-31. PMID: 15537298 DOI: 10.1021/jf049510t
Other literature(s)	N.D
PubDate	2004