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 - DFBPAMIC0519(Antimicrobial peptide)

DFBP ID	DFBPAMIC0519
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

Peptide mass

Experimental mass	Theoretical mass
1633 Da	1632.91 Da ^c

Net charge

Isoelectric point (pI)

11.54 ^c

IC₅₀

N.D

pIC₅₀

N.D

GRAVY

0.6267^c

Hydrophilic residue ratio

66.67%^c

Peptide calculator

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
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

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

Bitterness

Literature report	N.D
Bitter prediction tools	Non-bitter taste ^prediction

SMILES

N.D

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

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

[D1]

[D2]

[D3]

[D4]

Reference(s)

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. DOI: 10.1016/j.lwt.2020.109656
Other literature(s)	N.D
PubDate	2020