Abstract
Proline-rich antimicrobial peptides (PR-AMPs) have attracted much interest as they target Gram-negative and do not act by lytic mechanisms. In this study, a novel hybrid peptide OM19R was designed based on the Oncocin and MDAP-2. OM19R showed specific and improved potency against Escherichia coli (E. coli), Salmonella and Shigella standard strains compared to parental peptides. The minimum inhibitory concentrations (MICs) ranged from 1 to 2 μM. However, the activity against Klebsiella pneumoniae (K. pneumoniae) was inhibited. The dependence of the SbmA protein for OM19R activity was also studied by a gene-knockout strain. The confocal laser scanning microscopy further revealed that OM19R could rapidly penetrate into E. coli cells without membrane damage. In summary, the hybrid peptide OM19R is a strong cell-selective antibacterial peptide and a promising specific antibacterial agent.
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