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Antibacterial Activity and Mechanism of a Bacteriocin Derived from the Valine-Cecropin A(1–8)-Plantaricin ZJ5(1–18) Hybrid Peptide Against Escherichia coli O104

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Abstract

Peptide fragment hybridization is an effective method to obtain novel hybrid antimicrobial peptides with higher antibacterial activities. The novel peptide, valine-cecropin A(1–8)-plantaricin ZJ5(1–18) (CA-P), was designed by coupling the amphiphilic N-terminal fragment of CA with the N-terminal core helix of P and adding a valine residue to the N-terminus of the hybrid fragment. CA-P showed higher antibacterial activities than the parental peptide P against all indicator strains in the experiment, with no hemolytic activity against sheep red blood cells. Observations by scanning electron microscopy and transmission electron microscopy confirmed that CA-P destroyed the surface structure of the bacteria and caused leakage of the cellular contents. As determined by fluorescence microscopy, the antibacterial mechanism of CA-P is microorganism killing. It was observed that CA-P and Litsea mollis Hemsl. essential oil showed a significant synergistic effect against Salmonella enterica serovar Newport.

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Acknowledgements

This research was supported by the Natural Science Foundation of Zhejiang Province (No.LY18C06004) and Food Science and Engineering, the most important discipline of Zhejiang Province (No. JYTSP20142012).

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  1. Key Laboratory for Food Microbial Technology of Zhejiang Province, Zhejiang Gongshang University, #18, Xue zheng Street, 310018, Hangzhou, People’s Republic of China

    Yunzhi Jiang, Canchao Mei, Xi Huang, Qing Gu & Dafeng Song

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  1. Yunzhi Jiang
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Jiang, Y., Mei, C., Huang, X. et al. Antibacterial Activity and Mechanism of a Bacteriocin Derived from the Valine-Cecropin A(1–8)-Plantaricin ZJ5(1–18) Hybrid Peptide Against Escherichia coli O104. Food Biophysics 15, 442–451 (2020). https://doi.org/10.1007/s11483-020-09636-w

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