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 - DFBPACEI2095(ACE-inhibitory peptide)

DFBP ID	DFBPACEI2095
Peptide sequence	GYDTQAIVQ
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

Gly-Tyr-Asp-Thr-Gln-Ala-Ile-Val-Gln

Single-letter amino acid

GYDTQAIVQ

Peptide length

Peptide mass

Experimental mass	Theoretical mass
992.7431 Da	994.07 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

3.13 ^c

IC₅₀

1.0 mM (= 1000 μM)

pIC₅₀

0.0

GRAVY

-0.2667^c

Hydrophilic residue ratio

44.44%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Animal, Milk protein
Organism/Source	Bovine whey protein
Precursor protein	α-Lactalbumin
Residue position	f(54-62)
Precursor protein(s) search	Source.1: DFBPPR7685 ---- Milk proteins ---- Alpha-lactalbumin Source.2: DFBPPR7697 ---- Milk proteins ---- Alpha-lactalbumin Source.3: DFBPPR7711 ---- Milk proteins ---- Alpha-lactalbumin Source.4: DFBPPR8490 ---- Milk proteins ---- Alpha-lactalbumin
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 very weak Angiotensin-Converting Enzyme (ACE) (EC 3.4.15.1) inhibitory activity with an IC₅₀ value of 1.0 mM (= 1000 μM).
Specific target protein(s)	Specific Target Protein(s): Angiotensin-converting enzyme

Taste properties & Structure

Bitterness

Literature report	N.D
Bitter prediction tools	Non-bitter taste ^prediction

SMILES

NCC(=O)N[C@@]([H])(Cc1ccc(O)cc1)C(=O)N[C@@]([H])(CC(=O)O)C(=O)N[C@@]([H])([C@]([H])(O)C)C(=O)N[C@@]([H])(CCC(=O)N)C(=O)N[C@@]([H])(C)C(=O)N[C@@]([H])([C@]([H])(CC)C)C(=O)N[C@@]([H])(C(C)C)C(=O)N[C@@]([H])(CCC(=O)N)C(=O)O

Preparation method

Mode of preparation	Enzymatic hydrolysis
Enzyme(s)/starter culture	α-Lactalbumin was hydrolyzed with proteases from Bromelia antiacantha Bertol., a native plant.

Stability & Cytotoxicity

Peptide stability

Literature report:	GYDTQAIVQ in silico gastrointestinal digestion released two known ACE-inhibitory peptides (GY and IVQ). In these case, both GY (IC₅₀ = 210 μM) and IVQ peptides were more efficient ACE inhibitors than original peptide.
EHP-Tool:	Enzymatic Hydrolysis Prediction Tool (EHP-Tool)

Peptide cytotoxicity

Literature report:	In silico analysis indicated that the peptide was non-toxic (ToxinPred).
Prediction:	ToxinPred

Additional information

The results indicate that cysteine peptidases from B. antiacantha hydrolyse α-lactalbumin to produce novel ACE inhibitory peptides that could be useful even as functional food ingredients.

Database cross-references

[D1]

[D2]

[D3]

[D4]

Reference(s)

Primary literature	Villadóniga, C., Cantera, A.M.B. New ACE-inhibitory peptides derived from α-lactalbumin produced by hydrolysis with Bromelia antiacantha peptidases. Biocatalysis and Agricultural Biotechnology. 2019, 20. DOI: 10.1016/j.bcab.2019.101258
Other literature(s)	N.D
PubDate	2019