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(2020)
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.
MoreTranslated text
Key words
Hybrid peptide, Antibacterial activity, Valine-Cecropin A(1–8)-Plantaricin ZJ5(1–18), Mechanism, Synergistic effect
AI Read Science
Must-Reading Tree
Example
Generate MRT to find the research sequence of this paper
Chat Paper
Summary is being generated by the instructions you defined