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 - DFBPACEI0347(ACE-inhibitory peptide)

DFBP ID	DFBPACEI0347
Peptide sequence	TPVVVPPFLQP
Type	Native peptide
Peptide/Function name	ACE-inhibitory peptide

Function-activity relationship

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

Calculated physicochemical properties

Three-letter amino acid

Thr-Pro-Val-Val-Val-Pro-Pro-Phe-Leu-Gln-Pro

Single-letter amino acid

TPVVVPPFLQP

Peptide length

Peptide mass

Experimental mass	Theoretical mass
1193.6 Da	1193.45 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

5.97 ^c

IC₅₀

749 uM

pIC₅₀

-2.874

GRAVY

0.7818^c

Hydrophilic residue ratio

81.82%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Animal
Organism/Source	Milk protein
Precursor protein	β-Casein
Residue position	f(80-90)
Precursor protein(s) search	Source.1: DFBPPR7692 ---- Milk proteins ---- Beta-casein Source.2: DFBPPR7700 ---- Milk proteins ---- Beta-casein Source.3: DFBPPR7718 ---- Milk proteins ---- Beta-casein Source.4: DFBPPR8489 ---- Milk proteins ---- Beta-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 low Angiotensin-Converting Enzyme (ACE) (EC 3.4.15.1) inhibitory activity with an IC₅₀ value of 749 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])([C@]([H])(O)C)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(C(C)C)C(=O)N[C@@]([H])(C(C)C)C(=O)N[C@@]([H])(C(C)C)C(=O)N1[C@@]([H])(CCC1)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(Cc1ccccc1)C(=O)N[C@@]([H])(CC(C)C)C(=O)N[C@@]([H])(CCC(=O)N)C(=O)N1[C@@]([H])(CCC1)C(=O)O

Preparation method

Mode of preparation	Enzymatic hydrolysis
Enzyme(s)/starter culture	Whey protein was digested with Proteinase K at 37 ℃ for 24 h.

Stability & Cytotoxicity

Peptide stability

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

Peptide cytotoxicity

Literature report:	No measured
Prediction:	ToxinPred

Additional information

N.D

Database cross-references

DFBP

[D1]	DFBPANHY0551
[D2]	DFBPMUFU0105

[D3]

[D4]

[D5]

[D6]

Reference(s)

Primary literature	Abubakar, A., Saito, T., Kitazawa, H., Kawai, Y., Itoh, T. Structural analysis of new antihypertensive peptides derived from cheese whey protein by proteinase K digestion. J Dairy Sci. 1998, 81, 3131-8. DOI: 10.3168/jds.S0022-0302(98)75878-3
Other literature(s)	[1] Bösze Z. Bioactive Components of Milk[M]. Springer New York, 2008. [2] Martinez-Maqueda, D., et al., Antihypertensive peptides from food proteins: a review. Food Funct, 2012. 3(4): p. 350-61.
PubDate	1998