Design, synthesis and antibacterial activity of a novel hybrid antimicrobial peptide LFM23

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 solidphase 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 against Escherichia coli AT CC25922, Salmonella typhimurium ATCC12291, Pseudomonas aeruginosa ATCC27853, Staphylococcus aureus ATCC25923, Pichia pastoris GS115, 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 as clinically useful antimicrobial agents.

Mammals’ antimicrobial peptides: potential and limitations for the treatment of Staphylococcus aureus infections

“…Likewise, this influence of single amino acids on the overall effect of AMPs is also shown by the increase in antimicrobial activity caused by tryptophan addition; it is believed that tryptophan plays a role of anchor in membrane proteins and also helps the translocations of the AMP across the phospholipid bilayer 40 . Chain length and cyclization of the molecule, as well as amino acids substitution or position shifting, may also be related to reduced cytotoxicity and increased/maintained activity 27 , but require more investigation.…”