Abstract

Antimicrobial peptides (AMPs) are short and generally positively charged peptides found in a wide variety of organisms. CS alpha beta defensins are a group of AMPs. These defensins are composed of an alpha-helix and a beta-sheet linked by three or four disulphide bridges. In this study, we describe the antimicrobial activity of an anionic CS alpha beta fungal defensin from Aspergillus fumigatus, AfusinC. AfusinC was recombinantly produced as a fusion protein in Escherichia coll. The tag was removed by proteolytic cleavage, and AfusinC was purified by size exclusion chromatography. About 0.8 mg of recombinant AfusinC was obtained from 1 L of culture. Recombinant AfusinC was active against mainly gram-positive bacteria including human pathogens and a multiresistant-strain of A. aureus. Additionally, AfusinC showed bactericidal effect against Micrococcus luteus.