Abstract

Antimicrobial peptides produced by many tissues and cell types of invertebrates, insects and humans as part of their innate immune system, have received increasing attention as potential candidates due to their administration as pharmaceutical agents. In the present study, a novel hybrid antimicrobial peptide LFM23 consisting of 23 amino acid residues was designed based on the primary sequences of bovine lactoferricin (LfcinB) and melittin. The peptide was synthesized by chemical method of solid-phase synthesis with a purity of more than 98% after reverse phase high performance liquid chromatography. Antimicrobial activity assay showed that LFM23 had strong antibacterial abilities, and the minimum inhibitory concentrations againstEscherichia coli ATCC25922, Salmonella typhimurium ATCC12291, Pseudomonas aeruginosa ATCC27853, Staphylococcus aureus ATCC25923, Pichia pastorisGS115, were 32, 32, 64, 32 and 256 μg/ml, respectively. The hemolytic assays indicated that LFM23 had no hemolytic action in vitro at antimicrobial concentration. The results demonstrate that the peptide LFM23 has a good application prospect asclinically useful antimicrobial agents.

Key words: Antimicrobial peptides, design, LfcinB, melittin, antibacterial activity.