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List of peptide properties
DFBP ID - DFBPAMIC0519(Antimicrobial peptide)
Peptide sequence AWQKFLSAVVSALGR
Type Native peptide
Peptide/Function name Antimicrobial peptide, LCH4
Function-activity relationship
Main bioactivity Antimicrobial activity
Otheir bioactivity N.D
Calculated physicochemical properties
Three-letter amino acid Ala-Trp-Gln-Lys-Phe-Leu-Ser-Ala-Val-Val-Ser-Ala-Leu-Gly-Arg
Single-letter amino acid AWQKFLSAVVSALGR
Peptide length 15
Peptide mass
Experimental mass Theoretical mass
1633 Da 1632.91 Da c
Net charge +2
Isoelectric point (pI) 11.54 c
IC50 N.D
pIC50 N.D
GRAVY 0.6267 c
Hydrophilic residue ratio 60% c
Peptide calculator
To calculate the physicochemical properties of bioactive peptide.
Peptide source & Food-borne protein(s) search
Classification Animal, Marine fish
Organism/Source Large yellow croaker (Larimichthys crocea)
Precursor protein Hemoglobin
Residue position N.D
Precursor protein(s) search
No matching precursor protein found
There are no literature reports on the discovery of this sequence in other food-source proteins.
Biological/Functional activity & target protein
Antimicrobial activity

(1) The minimal inhibitory concentration (MIC) of LCH4 for S. aureus and V. parahaemolyticus was 12.5 μg/mL and 25 μg/mL, respectively.
(2) Transmission electron microscopy revealed that LCH4 killed bacteria by perforating their cell wall, resulting in the leakage of intracellular solutes and the consequent collapse of the cell membrane.
(3) LCH4 was able to increase the inner-membrane permeability of V. parahaemolyticus in a concentration-dependent manner and was also able to inhibit biofilm formation by S. aureus and V. parahaemolyticus by 88.0% and 75.0%, respectively, at 1 x MIC.

Specific target protein(s) N.D
Taste properties & Structure
Literature report N.D
Bitter prediction tools Non-bitter taste prediction
Preparation method
Mode of preparation Synthesis
Enzyme(s)/starter culture

Two online applications, Antibacterial peptides (AntiBP) and the Collection of Antimicrobial Peptides (CAMP) server, were used for the prediction of antimicrobial peptides derived from hemoglobin from L. crocea (GenBank: AAV91971.1). Peptides were then synthesized and purified by a commercial company, Scilight Biotechnology Co.

Stability & Cytotoxicity
Peptide stability
Literature report: N.D
EHP-Tool: Enzymatic Hydrolysis Prediction Tool (EHP-Tool)
Peptide cytotoxicity
Literature report:

The LCH4 peptide had no cytotoxic effects on normal human hepatocytes, even at high concentrations (16 x MIC), with a cell survival rate of more than 93%.

Prediction: ToxinPred
Additional information
Additional information

LCH4 had a strong inhibitory effect on the growth of pathogenic bacteria in soy sauce, which makes LCH4 a good candidate for broad application as a food preservative.

Database cross-references
APD [D2] -
BioPepDB [D3] -
MBPDB [D4] -
Primary literature Shen Y A , Yd A , JJ A B, et al. A hemoglobin-derived antimicrobial peptide, LCH4, from the large yellow croaker (Larimichthys crocea) with potential use as a food preservative - ScienceDirect[J]. LWT, 2020, 131.
Other literature(s) N.D
PubDate 2020
Copyright © 2020. Record / license number: Chongqing ICP No. 2000214