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 - DFBPACEI0057(ACE-inhibitory peptide)

DFBP ID	DFBPACEI0057
Peptide sequence	DKIHP
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

Asp-Lys-Ile-His-Pro

Single-letter amino acid

DKIHP

Peptide length

Peptide mass

Experimental mass	Theoretical mass
609.2 Da	608.69 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

7.76 ^c

IC₅₀

113.1 uM

pIC₅₀

-2.053

GRAVY

-1.5400^c

Hydrophilic residue ratio

40%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Animal
Organism/Source	Spanish cheeses (Manchego, Roncal, Idiazabal, Goat, Ovine, Cabrales), Ovine milk, Caprine milk
Precursor protein	β-Casein
Residue position	f(47-51)
Precursor protein(s) search	Source.1: DFBPPR1006 ---- Plant proteins ---- Cellulose synthase A catalytic subunit 4 [UDP-forming] Source.2: DFBPPR7692 ---- Milk proteins ---- Beta-casein Source.3: DFBPPR7700 ---- Milk proteins ---- Beta-casein Source.4: DFBPPR7718 ---- Milk proteins ---- Beta-casein Source.5: DFBPPR8489 ---- Milk proteins ---- Beta-casein Source.6: DFBPPR18496 ---- Animal proteins ---- Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase Source.7: DFBPPR15529 ---- Microorganism protein ---- Oleate activated transcription factor 3
Link-research Inductive analysis	Link 1: DFBPACEI1802----Manchego cheeses, Ovine milk protein----β-Casein

Biological/Functional activity & target protein

ACE-inhibitory activity	The peptide exhibited Angiotensin-Converting Enzyme (ACE) (EC 3.4.15.1) inhibitory activity with an IC₅₀ value of 113.1 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])(CC(=O)O)C(=O)N[C@@]([H])(CCCCN)C(=O)N[C@@]([H])([C@]([H])(CC)C)C(=O)N[C@@]([H])(CC1=CN=C-N1)C(=O)N1[C@@]([H])(CCC1)C(=O)O

Preparation method

Mode of preparation	Preparation of water-soluble-extract (WSE).
Enzyme(s)/starter culture	The WSEs were fractionated by passing them through a membrane with a molecular weight cut-off 1000 Da at 5 ◦C in a stirred-cell type ultrafiltration module, under a pressure of 3 bars applied with nitrogen (no enzyme).

Stability & Cytotoxicity

Peptide stability

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

Peptide cytotoxicity

Literature report:	N.D
Prediction:	ToxinPred

Additional information

(1) The casein fragment DKIHP showed ACE-inhibitory activity with an IC₅₀ of 113.1 μM but the addition of a phenylalanine residue at the C-terminal led to a dramatic decrease in the inhibitory activity (2419.4 μM). It is known that a proline residue in the penultimate position diminishes the interaction of this peptide with the enzyme^[7].
(2) The peptide can be obtained by two different synthetic procedures (Boc and Fmoc)^[4].

Database cross-references

[D1]

[D2]

[D3]

[D4]

Reference(s)

Primary literature	Gómez-Ruiz, J.Á., Taborda, G., Amigo, L., Recio, I., Ramos, M. Identification of ACE-inhibitory peptides in different Spanish cheeses by tandem mass spectrometry. European Food Research and Technology. 2006, 223, 595-601. DOI: 10.1007/s00217-005-0238-0
Other literature(s)	[1] Gómez-Ruiz J á, Recio I, Pihlanto A. Antimicrobial activity of ovine casein hydrolysates. A preliminary study[J]. Milchwissenschaft-milk Science International, 2005, 60(1):41-44. [2] Gomezruiz J A, Ramos M, Recio I. Angiotensin-converting enzyme-inhibitory peptides in Manchego cheeses manufactured with different starter cultures.[J]. International Dairy Journal, 2002, 12(8):697-706. [3] Papadimitriou C G, Vafopoulou-Mastrojiannaki A, Silva S V, et al. Identification of peptides in traditional and probiotic sheep milk yoghurt with angiotensin I-converting enzyme (ACE)-inhibitory activity[J]. Food Chemistry, 2007, 105(2):647-656. [4] Gómez-Ruiz J A, Recio I, Belloque J. ACE-inhibitory activity and structural properties of peptide Asp-Lys-Ile-His-Pro [beta-CN f(47-51)]. Study of the peptide forms synthesized by different methods[J]. J Agric Food Chem, 2004, 52(20):6315-9. [5] Quirós A, Hernándezledesma B, Ramos M, et al. Angiotensin-converting enzyme inhibitory activity of peptides derived from caprine kefir.[J]. Journal of Dairy Science, 2005, 88(10):3480-3487. [6] Park Y W. Bioactive Components in Milk and Dairy Products[M]. 2009. [7] Cheung H S , Wang F L , Ondetti M A , et al. Binding of peptide substrates and inhibitors of angiotensin-converting enzyme. Importance of the COOH-terminal dipeptide sequence.[J]. Journal of Biological Chemistry, 1980, 255(2):401-7.
PubDate	2006