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 - DFBPACEI0278(ACE-inhibitory peptide)

DFBP ID	DFBPACEI0278
Peptide sequence	PYVRYL
Type	Native peptide
Peptide/Function name	ACE-inhibitory peptide

Function-activity relationship

Main bioactivity	ACE-inhibitory activity
Otheir bioactivity	Antihypertensive activity ^[D1], Antioxidative activity ^[D2], Antimicrobial activity ^[D3], Multifunctional activity ^[D4]

Calculated physicochemical properties

Three-letter amino acid

Pro-Tyr-Val-Arg-Tyr-Leu

Single-letter amino acid

PYVRYL

Peptide length

Peptide mass

Experimental mass	Theoretical mass
809.3 Da	809.95 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

9.59 ^c

IC₅₀

2.4 ± 0.2 μM

pIC₅₀

-0.38

GRAVY

-0.1167^c

Hydrophilic residue ratio

50%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Animal
Organism/Source	Caprine milk protein, Caprine kefir
Precursor protein	α_s2-Casein
Residue position	f(203-208)
Precursor protein(s) search	Source.1: DFBPPR7689 ---- Milk proteins ---- Alpha-S2-casein Source.2: DFBPPR7701 ---- Milk proteins ---- Alpha-S2-casein Source.3: DFBPPR8494 ---- Milk proteins ---- Alpha-S2-casein
Link-research Inductive analysis	Link 1: DFBPACEI1727----Ovine milk protein----α_s2-Casein

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 2.4 ± 0.2 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

N1[C@@]([H])(CCC1)C(=O)N[C@@]([H])(Cc1ccc(O)cc1)C(=O)N[C@@]([H])(C(C)C)C(=O)N[C@@]([H])(CCCNC(=N)N)C(=O)N[C@@]([H])(Cc1ccc(O)cc1)C(=O)N[C@@]([H])(CC(C)C)C(=O)O

Preparation method

Mode of preparation	Fermentation
Enzyme(s)/starter culture	Kefir was prepared using pasteurized milk cultured with kefir grains that contained the lactic acid bacteria Lactococcus lactis, Lactococcus cremoris, Lactococcus biovar. diacetylactis, Leuconostoc mesenteroides ssp. cremoris, Lactobacillus plantarum, Lactobacillus casei, and the yeast Kluyveromyces marxianus var. fragilis (Torula kefir).

Stability & Cytotoxicity

Peptide stability

Literature report:

The peptide PYVRYL was not resistant to the incubation with pepsin followed by hydrolysis with Corolase PP.

Table 1. Behavior of angiotensin-converting enzyme (ACE)-inhibitory activity of peptides obtained from 3-kDa permeate of caprine kefir-water soluble extract under simulation of gastrointestinal digestion. Sequence and ACE-inhibitory activity of peptides released after digestion.
Sequence	IC₅₀, mg/mL ^a		Degree of hydrolysis	Fragments released after digestion
	Before digestion	After digestion
PYVRYL	0.002 ± 0.0001	0.086 ± 0.009	Hydrolyzed	PYV
^a Concentration of peptide needed to inhibit 50% the original ACE activity. Results are presented as the mean (n = 3) ± SD.

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]	DFBPANHY0547
[D2]	DFBPANOX0715
[D3]	DFBPAMIC0185
[D4]	DFBPMUFU0387

BIOPEP-UWM

[D5]

8152, 8178, 8262

APD

[D6]

BioPepDB

[D7]

MBPDB

[D8]

Reference(s)

Primary literature	Quirós, A., Hernández-Ledesma, B., Ramos, M., Amigo, L., Recio, I. Angiotensin-Converting Enzyme Inhibitory Activity of Peptides Derived from Caprine Kefir. Journal of Dairy Science. 2005, 88, 3480-7. DOI: 10.3168/jds.S0022-0302(05)73032-0
Other literature(s)	[1] Lopez E I, Recio I. Antibacterial activity of peptides and folding variants from milk proteins[J]. International Dairy Journal, 2006, 16(11):1294-1305. [2] López-Expósito I, Quirós A, Amigo L, et al. Casein hydrolysates as a source of antimicrobial, antioxidant and antihypertensive peptides[J]. Dairy Science & Technology, 2007, 87(4):241-249. [3] Park Y W. Bioactive Components in Milk and Dairy Products[M]. 2009. [4] Recio I., Quirós A., Hernández-Ledesma, B., Gómez-Ruiz, J.A, Miguel, M., Amigo, L., López- Expósito, I., Ramos, M., and Aleixandre A. 2005. Bioactive peptides identified in enzyme hydro- lysates from milk caseins and procedure for their obtention. European Patent PCT/ ES2006070079. [5] LóPezexpóSito I, Gomezruiz J A, Amigo L, et al. Identification of antibacterial peptides from ovine αs2-casein[J]. International Dairy Journal, 2006, 16(9):1072-1080.
PubDate	2005