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 - DFBPACEI2094(ACE-inhibitory peptide)

DFBP ID	DFBPACEI2094
Peptide sequence	TTFHTSGY
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

Thr-Thr-Phe-His-Thr-Ser-Gly-Tyr

Single-letter amino acid

TTFHTSGY

Peptide length

Peptide mass

Experimental mass	Theoretical mass
912.4132 Da	912.95 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

7.74 ^c

IC₅₀

142 μM

pIC₅₀

-2.152

GRAVY

-0.6250^c

Hydrophilic residue ratio

25%^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(48–55)
Precursor protein(s) search	Source.1: 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 potent Angiotensin-Converting Enzyme (ACE) (EC 3.4.15.1) inhibitory activity with an IC₅₀ value of 142 μM. Inhibition kinetic analysis showed that TTFHTSGY was a fully functional ACE competitive inhibitor.
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

N[C@@]([H])([C@]([H])(O)C)C(=O)N[C@@]([H])([C@]([H])(O)C)C(=O)N[C@@]([H])(Cc1ccccc1)C(=O)N[C@@]([H])(CC1=CN=C-N1)C(=O)N[C@@]([H])([C@]([H])(O)C)C(=O)N[C@@]([H])(CO)C(=O)NCC(=O)N[C@@]([H])(Cc1ccc(O)cc1)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:	TTFHTSGY in silico gastrointestinal digestion released ACE inhibitory dipeptides TF and SG. TF was shown to have more potent ACE-inhibitory effect (IC₅₀ = 18 μM) 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