A potential food biopreservative, CecXJ-37N, non-covalently intercalates into the nucleotides of bacterial genomic DNA beyond membrane attack

•CecXJ-37N shows small MICs (0.25–7.8μM) against 8 food-borne pathogenic strains.•CecXJ-37N shows low hemolysis and no cytotoxicity to normal mammalian cells.•CecXJ-37N induces pore-forming on E. coli cell membrane and causes cytolysis.•CecXJ-37N penetrates bacterial cell membrane and interacts with...

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Bibliographic Details
Published in:Food chemistry Vol. 217; pp. 576 - 584
Main Authors: Liu, Dongliang, Liu, Jun, Li, Jinyao, Xia, Lijie, Yang, Jianhua, Sun, Surong, Ma, Ji, Zhang, Fuchun
Format: Journal Article
Language:English
Published: England Elsevier Ltd 15.02.2017
Subjects:
Amide modification
Animals
Anti-Bacterial Agents - chemistry
Anti-Bacterial Agents - pharmacology
antibacterial properties
Antimicrobial Cationic Peptides - chemistry
Antimicrobial Cationic Peptides - pharmacology
Antimicrobial peptide
Cell Membrane - drug effects
Cell membrane penetration
Cell Survival - drug effects
cytoplasm
cytotoxicity
DNA
DNA intercalation
DNA, Bacterial - chemistry
Escherichia coli
Escherichia coli - drug effects
flow cytometry
fluorescence microscopy
food biopreservatives
Food Contamination - prevention & control
food industry
Food Microbiology
Food preservative
Food Preservatives - chemistry
Food Preservatives - pharmacology
Food-borne pathogen
genome
Genome, Bacterial
hydrolysis
mechanism of action
Mice
Microbial Sensitivity Tests
Molecular Structure
NIH 3T3 Cells
novel foods
nucleotides
pepsin
scanning electron microscopy
trypsin
ultraviolet-visible spectroscopy
Food preservative
Cell membrane penetration
Food-borne pathogen
Amide modification
DNA intercalation
Antimicrobial peptide
ISSN:0308-8146, 1873-7072, 1873-7072
Online Access:Get full text
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Summary:•CecXJ-37N shows small MICs (0.25–7.8μM) against 8 food-borne pathogenic strains.•CecXJ-37N shows low hemolysis and no cytotoxicity to normal mammalian cells.•CecXJ-37N induces pore-forming on E. coli cell membrane and causes cytolysis.•CecXJ-37N penetrates bacterial cell membrane and interacts with genomic DNA.•CecXJ-37N intercalates into nucleotides rather than binds to DNA backbone. The antibacterial activities and mechanism of an amide-modified peptide CecXJ-37N were investigated in this study. CecXJ-37N showed small MICs (0.25–7.8μM) against eight harmful strains common in food industry. The α-helix proportion of CecXJ-37N increased by 11-fold in prokaryotic membrane comparable environments; cytotoxicity studies demonstrated the MHC was significantly higher than that of non-amidated isoform. Moreover, CecXJ-37N possessed stronger capacities to resist trypsin and pepsin hydrolysis within two hours. Flow cytometry and scanning electron microscopy demonstrated that CecXJ-37N induced pore-formation, morphological changes, and lysed E. coli cells. Fluorescence microscopy indicated that CecXJ-37N penetrated E. coli membrane and accumulated in cytoplasm. Further ultraviolet–visible spectroscopy suggested that CecXJ-37N changed the action mode of parental peptide interacting with bacterial genome from outside binding to a tightly non-covalent intercalation into nucleotides. Overall, this study suggested that amide-modification enhanced antimicrobial activity and reduced the cytotoxicity, thus could be potential strategies for developing novel food preservatives.
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ISSN:0308-8146
1873-7072
1873-7072
DOI:10.1016/j.foodchem.2016.09.033