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 - DFBPACEI1862(ACE-inhibitory peptide)

DFBP ID	DFBPACEI1862
Peptide sequence	LAPSLPGKPKPD
Type	Native peptide
Peptide/Function name	ACE-inhibitory peptide

Function-activity relationship

Main bioactivity	ACE-inhibitory activity
Otheir bioactivity	Antioxidative activity ^[D1], DPP IV-inhibitory activity ^[D2], α-Glucosidase inhibitory activity ^[D3], Multifunctional activity ^[D4]

Calculated physicochemical properties

Three-letter amino acid

Leu-Ala-Pro-Ser-Leu-Pro-Gly-Lys-Pro-Lys-Pro-Asp

Single-letter amino acid

LAPSLPGKPKPD

Peptide length

Peptide mass

Experimental mass	Theoretical mass
1219.701 Da	1219.42 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

9.84 ^c

IC₅₀

1.97 umol/L

pIC₅₀

-0.294

GRAVY

-0.7917^c

Hydrophilic residue ratio

66.67%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Animal
Organism/Source	Egg
Precursor protein	Egg-yolk protein by-product
Residue position	N.D
Precursor protein(s) search	Source.1: DFBPPR10968 ---- Animal proteins ---- Visual system homeobox 2
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 strong Angiotensin-Converting Enzyme (ACE) (EC 3.4.15.1) inhibitory activity with an IC₅₀ value of 1.97 umol/L.
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])(C)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(CO)C(=O)N[C@@]([H])(CC(C)C)C(=O)N1[C@@]([H])(CCC1)C(=O)NCC(=O)N[C@@]([H])(CCCCN)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(CCCCN)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(CC(=O)O)C(=O)O

Preparation method

Mode of preparation	Enzymatic hydrolysis
Enzyme(s)/starter culture	Enzymatic hydrolysis conducted using unconventional enzyme from Cucurbita ficifolia (dose: 1000 U/mg of hydrolyzed egg-yolk protein (E/S (w/w) = 1:7.52)) was employed to obtain protein hydrolysates. The 4-h hydrolysate exhibited a significant (IC₅₀ = 482.5 μg/mL) ACE inhibitory activity.

Stability & Cytotoxicity

Peptide stability

Literature report:	N.D
EHP-Tool:	Enzymatic Hydrolysis Prediction Tool (EHP-Tool)

Peptide cytotoxicity

Literature report:

The MTT assay results indicated that Egg-yolk protein hydrolysate used in concentrations of 1% and 10% did not show toxicity to animal and human cell lines during 48 h of incubation. Moreover, it may slightly affect the growth of Balb 3T3 cell lines, as shown in Table 1.

Table 1. Cytotoxic/proliferation activity of egg yolk protein hydrolysate obtained with using a serine proteinase from *C. ficifolia* (1000 U/mg of hydrolyzed Egg-yolk protein (E:S (w/w) = 1:7.52). Tested cell lines: mouse fibroblasts (Balb3T3), human hepatocytes (HepG2) and human keratinocytes (HaCaT). All data were expressed as mean values (mean ± SD, n = 3).
Hydrolysate	MTT test A 560 nm
Hydrolysate	Balb 3T3	HepG2	HaCaT
0	0.07 ± 0.01	0.17 ± 0.04	0.05 ± 0.02
1	0.07 ± 0.02	0.17 ± 0.03	0.05 ± 0.01
10	0.13 ± 0.02	0.17 ± 0.02	0.05 ± 0.02

Prediction:

ToxinPred

Additional information

Egg-yolk protein hydrolysate showed no cytotoxic activity on human and animal cell lines which makes it a very useful multifunctional method for peptide preparation. The research indicates the possibility of using of Egg-yolk protein hydrolysate as additive in functional foods, pharmacological substances or cosmetics.

Database cross-references

DFBP

[D1]	DFBPANOX0390
[D2]	DFBPDPIV0031
[D3]	DFBPALGL0020
[D4]	DFBPMUFU0571

BIOPEP-UWM

[D5]

8388, 8547, 8548, 8550

APD

[D6]

BioPepDB

[D7]

MBPDB

[D8]

Reference(s)

Primary literature	Eckert E, Zambrowicz A, Pokora M, Setner B, Dąbrowska A, Szołtysik M, Szewczuk Z, Polanowski A, Trziszka T, Chrzanowska J. Egg-yolk protein by-product as a source of ACE-inhibitory peptides obtained with using unconventional proteinase from Asian pumpkin (Cucurbita ficifolia). J Proteomics. 2014 Oct 14;110:107-16. PMID: 25138009 DOI: 10.1016/j.jprot.2014.08.003
Other literature(s)	[1] Aleksandra Zambrowicz, Ewelina Eckert, Marta Pokora, et al. Antioxidant and antidiabetic activities of peptides isolated from a hydrolysate of an egg-yolk protein by-product prepared with a proteinase from Asian pumpkin (Cucurbita ficifolia)[J]. RSC Advances, 2015, 5(14):10460-10467.
PubDate	2014