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List of peptide properties
DFBP ID - DFBPACEI1368(ACE-inhibitory peptide)
DFBP ID DFBPACEI1368
Peptide sequence DYVGN
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-Tyr-Val-Gly-Asn
Single-letter amino acid DYVGN
Peptide length 5
Peptide mass
Experimental mass Theoretical mass
N.D 566.57 Da c
Net charge 0.00 c
Isoelectric point (pI) 3.13 c
IC50 0.72 uM
pIC50 0.143
GRAVY -0.9000 c
Hydrophilic residue ratio 40% c
Peptide calculator
To calculate the physicochemical properties of bioactive peptide.
Peptide source & Food-borne protein(s) search
Classification Plant
Organism/Source Wheat
Precursor protein Wheat germ hydrolysates
Residue position N.D
Precursor protein(s) search
Link-research
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 strong Angiotensin-Converting Enzyme (ACE) (EC 3.4.15.1) inhibitory activity with an IC50 value of 0.72 μM.

Specific target protein(s) Specific Target Protein(s):
Angiotensin-converting enzyme
Taste properties & Structure
Bitterness
Literature report N.D
Bitter prediction tools Non-bitter taste prediction
SMILES N[C@@]([H])(CC(=O)O)C(=O)N[C@@]([H])(Cc1ccc(O)cc1)C(=O)N[C@@]([H])(C(C)C)C(=O)NCC(=O)N[C@@]([H])(CC(=O)N)C(=O)O
Preparation method
Mode of preparation

Enzymatic hydrolysis

Enzyme(s)/starter culture

The hydrolyzate with the most potent ACE inhibitory activity was obtained by 0.5 wt.%–8 h Bacillus licheniformis alkaline protease hydrolysis after 3.0 wt.%–3 h α-amylase treatment of defatted WG (IC50: 0.37 mg protein ml−1).

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
Additional information

The purified peptide DYVGN is a possible candidate for application as a dietary supplement or as a component of a functional food product.

Database cross-references
BIOPEP-UWM [D1] -
APD [D2] -
BioPepDB [D3] -
MBPDB [D4] -
Reference(s)
Primary literature Matsui T, Li CH, Osajima Y. Preparation and characterization of novel bioactive peptides responsible for angiotensin I-converting enzyme inhibition from wheat germ. J Pept Sci. 1999 Jul;5(7):289-97.
PMID: 10442764
Other literature(s) N.D
PubDate 1999
Copyright © 2020. Record / license number: Chongqing ICP No. 2000214