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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Vydáno v:Food chemistry Ročník 217; s. 576 - 584
Hlavní autoři: Liu, Dongliang, Liu, Jun, Li, Jinyao, Xia, Lijie, Yang, Jianhua, Sun, Surong, Ma, Ji, Zhang, Fuchun
Médium: Journal Article
Jazyk:angličtina
Vydáno: England Elsevier Ltd 15.02.2017
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ISSN:0308-8146, 1873-7072, 1873-7072
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Shrnutí:•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.
Bibliografie:ObjectType-Article-1
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ISSN:0308-8146
1873-7072
1873-7072
DOI:10.1016/j.foodchem.2016.09.033