High-level expression of a hybrid antimicrobial peptide LfcinB-Cecropin in Escherichia coli and its activity

Abstract:

[Objective] Resistant strains have become increasingly prominent issues, and the development of safe and efficient antimicrobial agents becomes the focus one of researches so far. Antimicrobial peptides possess many attractive features. Exploration and recombinant expression of antimicrobial peptides with high activity have important significance for solving resistant strains problem. [Methods] A novel hybrid antimicrobial peptide LfcinB-Cecropin was designed based on the structures of LfcinB and Cecropin. The gene encoding LfcinB-Cecropin was synthesized according to codon preference of E. coli. Tandem expression plasmids contained multicopy tandem LfcinB-Cecropin genes were constructed by the method of isocaudarner, and expressed them in E. coli. [Results] LfcinB-Cecropin was successfully expressed as fusion protein by IPTG induction. After sonication, inclusion body purification, formic acid cleavage, the recombinant LfcinB-Cecropin was obtained and showed obvious antibacterial activity. [Conclusion] A novel antimicrobial peptide LfcinB-Cecropin was obtained and recombinantly expressed in E. coli in high level.