Design, expression, and characterization of the hybrid antimicrobial peptide T-catesbeianin-1 based on FyuA.

The overuse of antibiotics has resulted in the emergence of antibiotic-resistant bacteria, which presents an urgent need for new antimicrobial agents. At present, antimicrobial peptides have attracted a great deal of attention from researchers. However, antimicrobial peptides often affect a broad range of microorganisms, including the normal flora in a host organism. In the present study, we designed a novel hybrid antimicrobial peptide, expressed the hybrid peptide, and studied its specific target. The hybrid peptide, named T-catesbeianin-1, which includes the FyuA-binding domain of pesticin and the peptide catesbeianin-1, was designed and expressed in Pichia pastoris X-33. Then, we determined the antimicrobial activity, cytotoxicity, and specific target of the peptide. T-catesbeianin-1 has strong antimicrobial activity and binds to FyuA to inhibit or kill Escherichia coli present in clinical specimens and mixed-species culture. In summary, these findings suggested that T-catesbeianin-1 might be promising and specific antibiotic agent for therapeutic application against fyuA E. coli.