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In this study we used a yeast expression system to express a new antimicrobial peptide dybowskin- 2CAMa from the skin cDNA library of Rana amurenisis. The entire coding region of the dybowskin-2CAMa was cloned into the plasmid pPICZα-A and then transformed into competent P. pastoris X33. The expressed dybowskin- 2CAMa was purified from the culture supernatant by Sephadex G-25 and YMC*GEL ODS-A chromatography followed by C18 reverse phased HPLC. The purified peptide exhibited a single band of about 2 kDa when resolved by Tricine-SDS-PAGE. Its exact molecular weight was 2456.46 Da which was consistent with the value predicted from its deduced amino acid sequence. Antimicrobial activity assay showed that the recombinant dybowskin- 2CAMa could inhibit the growth of a broad spectrum of bacteria, while displaying very low level of hemolytic activity (≤4% relative to Triton X-100), even at concentration of up to 500 µg/mL.

Expression of Antimicrobial Peptide Dybowskin-2CAMa in <em>Pichia pastoris</em> and Characterization of its Antibacterial Activity