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List of peptide properties
DFBP ID - DFBPAMIC0514(Antimicrobial peptide)
DFBP ID DFBPAMIC0514
Peptide sequence GLSDGEWQ
Type Native peptide
Peptide/Function name Antimicrobial peptide
Function-activity relationship
Main bioactivity Antimicrobial activity
Otheir bioactivity ACE-inhibitory activity [D1], Anticancer activity [D2], Multifunctional activity [D3]
Calculated physicochemical properties
Three-letter amino acid Gly-Leu-Ser-Asp-Gly-Glu-Trp-Gln
Single-letter amino acid GLSDGEWQ
Peptide length 8
Peptide mass
Experimental mass Theoretical mass
N.D 890.90 Da c
Net charge 0.00 c
Isoelectric point (pI) 3.04 c
IC50 N.D
pIC50 N.D
GRAVY -1.1500 c
Hydrophilic residue ratio 50% c
Peptide calculator
To calculate the physicochemical properties of bioactive peptide.
Peptide source & Food-borne protein(s) search
Classification Animal
Organism/Source Beef sarcoplasmic
Precursor protein Beef sarcoplasmic protein 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
Antimicrobial activity

Table 1 show the effects of ACE inhibitory peptide GLSDGEWQ on three Gram-positive (B. cereus, L. monocytogens, and S. aureus) and three Gram-negative (S. Typhimurium, E. Coli, and P. aeruginosa) pathogens. This peptide showed growth inhibition on Salmonella Typhimurium, Bacillus cereus, Escherichia coli, and Listeria monocytogenes at a 100 ppm level but not on Staphylococcus aureus and Pseudomonas aeruginosa.

Table 1. Antimicrobial activity of the synthetic peptide GLSDGEWQ on six pathogens
Concentration (μg)
Microorganisms
S. Typhimurium
B. cereus
E. coli
L. monoytogenes
S. aureus
P. aeruginosa
100
+
+++

200
++++

400
++++

+, Sensitive (9–12 mm inhibition); –, not detected.
Specific target protein(s) N.D
Taste properties & Structure
Bitterness
Literature report N.D
Bitter prediction tools Non-bitter taste prediction
SMILES NCC(=O)N[C@@]([H])(CC(C)C)C(=O)N[C@@]([H])(CO)C(=O)N[C@@]([H])(CC(=O)O)C(=O)NCC(=O)N[C@@]([H])(CCC(=O)O)C(=O)N[C@@]([H])(CC(=CN2)C1=C2C=CC=C1)C(=O)N[C@@]([H])(CCC(=O)N)C(=O)O
Preparation method
Mode of preparation Enzymatic hydrolysis
Enzyme(s)/starter culture

Hydrolysis with commercial enzymes (thermolysin+proteinase A).

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 ACE inhibitory peptides identified from beef sarcoplasmic protein hydrolysates have both antimicrobial and cancer cell cytotoxic effects. The ACE inhibitory peptides can be expected to possess other biological functions and used as functional materials for food industry.

Database cross-references
DFBP
[D1] DFBPACEI0115
[D2] DFBPANCA0332
[D3] DFBPMUFU0049
BIOPEP-UWM [D4] -
APD [D5] -
BioPepDB [D6] -
MBPDB [D7] -
Reference(s)
Primary literature Jang, A., Jo, C., Kang, K.-S., Lee, M. Antimicrobial and human cancer cell cytotoxic effect of synthetic angiotensin-converting enzyme (ACE) inhibitory peptides. Food Chem. 2008, 107, 327-36.
Other literature(s) N.D
PubDate 2008
Copyright © 2020. Record / license number: Chongqing ICP No. 2000214