Design, recombinant expression, and antibacterial activity of the cecropins-melittin hybrid antimicrobial peptides

Curr Microbiol. 2010 Sep;61(3):169-75. doi: 10.1007/s00284-010-9592-7. Epub 2010 Jan 29.

Abstract

In order to evaluate their antibacterial activities and toxicities, the cecropins-melittin hybrid antimicrobial peptide, CA(1-7)-M(4-11) (CAM) and CB(1-7)-M(4-11) (CBM), were designed by APD2 database. The recombinant hybrid antimicrobial peptides were successfully expressed and purified in Pichia pastoris. Antimicrobial activity assay showed that both of the two hybrid antimicrobial peptides had strong antibacterial abilities against Escherichia coli, Staphylococcus aureus, Pseudomonas aeruginosa, Klebsiella pneumoniae, Bacillus subtilis, Bacillus thuringiensis, and Salmonella derby. The potency of CAM and CBM to E. coli 25922 were 0.862 and 0.849, respectively, slightly lower than Amp's 0.957. The hemolytic assays indicated CAM and CBM had no hemolytic in vivo and in vitro, and so they had a good application prospect.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Anti-Infective Agents / metabolism
  • Anti-Infective Agents / pharmacology*
  • Bacteria / drug effects*
  • Cecropins / genetics
  • Cecropins / pharmacology*
  • Cecropins / toxicity
  • Erythrocytes / drug effects
  • Gene Expression*
  • Hemolysis
  • Melitten / genetics
  • Melitten / pharmacology*
  • Melitten / toxicity
  • Mice
  • Microbial Sensitivity Tests
  • Pichia / genetics
  • Pichia / metabolism
  • Recombinant Fusion Proteins / genetics
  • Recombinant Fusion Proteins / pharmacology
  • Recombinant Fusion Proteins / toxicity

Substances

  • Anti-Infective Agents
  • Cecropins
  • Recombinant Fusion Proteins
  • Melitten