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 - DFBPACEI0350(ACE-inhibitory peptide)

DFBP ID	DFBPACEI0350
Peptide sequence	YIPIQYVLSR
Type	Native peptide
Peptide/Function name	ACE-inhibitory peptide, Casokisin C

Function-activity relationship

Main bioactivity	ACE-inhibitory activity
Otheir bioactivity	Immunomodulatory activity ^[D1], Opioid activity ^[D2], Ileum contracting activity ^[D3], Multifunctional activity ^[D4]

Calculated physicochemical properties

Three-letter amino acid

Tyr-Ile-Pro-Ile-Gln-Tyr-Val-Leu-Ser-Arg

Single-letter amino acid

YIPIQYVLSR

Peptide length

Peptide mass

Experimental mass	Theoretical mass
N.D	1251.47 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

9.59 ^c

IC₅₀

100 uM

pIC₅₀

-2.0

GRAVY

0.4000^c

Hydrophilic residue ratio

50%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Animal
Organism/Source	Milk protein
Precursor protein	κ-Casein
Residue position	N.D
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 exhibited potent Angiotensin-Converting Enzyme (ACE) (EC 3.4.15.1) inhibitory activity with an IC₅₀ value of 100 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])(Cc1ccc(O)cc1)C(=O)N[C@@]([H])([C@]([H])(CC)C)C(=O)N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])([C@]([H])(CC)C)C(=O)N[C@@]([H])(CCC(=O)N)C(=O)N[C@@]([H])(Cc1ccc(O)cc1)C(=O)N[C@@]([H])(C(C)C)C(=O)N[C@@]([H])(CC(C)C)C(=O)N[C@@]([H])(CO)C(=O)N[C@@]([H])(CCCNC(=N)N)C(=O)O

Preparation method

Mode of preparation	Enzymatic hydrolysis
Enzyme(s)/starter culture	Hydrolysis with Trypsin.

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]	DFBPIMMU0051
[D2]	DFBPOPIO0004
[D3]	DFBPICPE0002
[D4]	DFBPMUFU0107

BIOPEP-UWM

[D5]

3213, 3215, 3216, 3495

APD

[D6]

BioPepDB

[D7]

MBPDB

[D8]

Reference(s)

Primary literature	Saito, T., Nakamura, T., Kitazawa, H., Kawai, Y., Itoh, T. Isolation and Structural Analysis of Antihypertensive Peptides That Exist Naturally in Gouda Cheese. Journal of Dairy Science. 2000, 83, 1434-40. DOI: 10.3168/jds.S0022-0302(00)75013-2
Other literature(s)	[1] Bösze Z. Bioactive Components of Milk[M]. Springer New York, 2008.
PubDate	2000