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 - DFBPACEI0291(ACE-inhibitory peptide)

DFBP ID	DFBPACEI0291
Peptide sequence	MAIPPKK
Type	Native peptide
Peptide/Function name	ACE-inhibitory peptide

Function-activity relationship

Main bioactivity	ACE-inhibitory activity
Otheir bioactivity	Antihypertensive activity ^[D1], Antithrombotic activity ^[D2], Multifunctional activity ^[D3]

Calculated physicochemical properties

Three-letter amino acid

Met-Ala-Ile-Pro-Pro-Lys-Lys

Single-letter amino acid

MAIPPKK

Peptide length

Peptide mass

Experimental mass	Theoretical mass
N.D	784.02 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

10.59 ^c

IC₅₀

N.D

pIC₅₀

N.D

GRAVY

-0.4000^c

Hydrophilic residue ratio

71.43%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Animal
Organism/Source	Ovine milk protein
Precursor protein	κ-Casein
Residue position	f(106-112)
Precursor protein(s) search	Source.1: DFBPPR7686 ---- Milk proteins ---- Kappa-casein Source.2: DFBPPR7695 ---- Milk proteins ---- Kappa-casein Source.3: DFBPPR7715 ---- Milk proteins ---- Kappa-casein Source.4: DFBPPR8492 ---- Milk proteins ---- Kappa-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 MAIPPKK was found to exhibit only moderate Angiotensin-Converting Enzyme (ACE) (EC 3.4.15.1) inhibitory activity levels at concentrations of up to 4785 μM (27% ACE inhibition).
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])(CCSC)C(=O)N[C@@]([H])(C)C(=O)N[C@@]([H])([C@]([H])(CC)C)C(=O)N1[C@@]([H])(CCC1)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(CCCCN)C(=O)N[C@@]([H])(CCCCN)C(=O)O

Preparation method

Mode of preparation	Enzymatic hydrolysis
Enzyme(s)/starter culture	Ovine milk proteins were hydrolyzed with L-1-tosylamide-2-phenylethyl chloromethyl ketone (TPCK)–treated trypsin (EC 3.4.21.4.) from the bovine pancreas (T-1426, Sigma Chemical Co., St. Louis, Mo.) with an enzyme/substrate ratio of 1/50 (wt/wt).

Stability & Cytotoxicity

Peptide stability

Literature report:	The peptide MAIPPKK was also subjected to the simulation of gastrointestinal conditions, and it was confirmed that its activity levels increased, especially during the first 90 min of hydrolysis with pepsin.
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]	DFBPANHY0543
[D2]	DFBPANTH0006, DFBPANTH0053, DFBPANTH0162
[D3]	DFBPMUFU0393

[D4]

[D5]

[D6]

[D7]

Reference(s)

Primary literature	Manso MA, López-Fandiño R. Angiotensin I converting enzyme-inhibitory activity of bovine, ovine, and caprine kappa-casein macropeptides and their tryptic hydrolysates. J Food Prot. 2003 Sep;66(9):1686-92. PMID: 14503726 DOI: 10.4315/0362-028X-66.9.1686
Other literature(s)	[1] Park Y W. Bioactive Components in Milk and Dairy Products[M]. 2009. [2] 2007 [3] W001-2012-017 [4] W001-2011-011
PubDate	2003