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 - DFBPACEI0361(ACE-inhibitory peptide)

DFBP ID	DFBPACEI0361
Peptide sequence	VAGTWY
Type	Native peptide
Peptide/Function name	ACE-inhibitory peptide

Function-activity relationship

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

Calculated physicochemical properties

Three-letter amino acid

Val-Ala-Gly-Thr-Trp-Tyr

Single-letter amino acid

VAGTWY

Peptide length

Peptide mass

Experimental mass	Theoretical mass
696 Da	695.77 Da ^c

Net charge

0.00 ^c

Isoelectric point (pI)

5.92 ^c

IC₅₀

1682 uM

pIC₅₀

-3.226

GRAVY

0.4500^c

Hydrophilic residue ratio

66.67%^c

Peptide calculator

Peptide source & Food-borne protein(s) search

Classification	Animal
Organism/Source	Milk whey protein
Precursor protein	β-Lactoglobulin
Residue position	f(15-20)
Precursor protein(s) search	Source.1: DFBPPR7687 ---- Milk proteins ---- Beta-lactoglobulin Source.2: DFBPPR7714 ---- Milk proteins ---- Beta-lactoglobulin Source.3: DFBPPR8499 ---- Milk proteins ---- Beta-lactoglobulin
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 very low Angiotensin-Converting Enzyme (ACE) (EC 3.4.15.1) inhibitory activity with an IC₅₀ value of 1682 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(C)C)C(=O)N[C@@]([H])(C)C(=O)NCC(=O)N[C@@]([H])([C@]([H])(O)C)C(=O)N[C@@]([H])(CC(=CN2)C1=C2C=CC=C1)C(=O)N[C@@]([H])(Cc1ccc(O)cc1)C(=O)O

Preparation method

Mode of preparation	Fermentation and enzymatic hydrolysis
Enzyme(s)/starter culture	Whey and casein proteins were fermented with lactic acid bacteria and hydrolysed subsequently by digestive enzymes (pepsin and 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]	DFBPANOX0699
[D2]	DFBPAMIC0336
[D3]	DFBPDPIV0025
[D4]	DFBPMUFU0111

BIOPEP-UWM

[D5]

3509, 4014, 8498, 8523, 9435

APD

[D6]

BioPepDB

[D7]

MBPDB

[D8]

Reference(s)

Primary literature	Pihlanto-Leppälä, A., Rokka, T., Korhonen, H. Angiotensin I Converting Enzyme Inhibitory Peptides Derived from Bovine Milk Proteins. International Dairy Journal. 1998, 8, 325-31. DOI: 10.1016/S0958-6946(98)00048-X
Other literature(s)	[1] Bösze Z. Bioactive Components of Milk[M]. Springer New York, 2008. [2] Pihlanto-Leppälä A, Koskinen P, Piilola K, et al. Angiotensin I-converting enzyme inhibitory properties of whey protein digests: concentration and characterization of active peptides[J]. Journal of Dairy Research, 2000, 67(1):53.
PubDate	1998