Abstract: Primary structure analyzing and secondary structure predicting indicate that BmKBPP of NDBPs (Non－Disulfide－Bridged Peptides) might be a polycovalent cationic host defense peptide, which has a typical structure of amphiphilic α－helix and plenty of basic amino acids(Arg and Lys)with net positive charges. Using PCR method and plasmid vector pGEX－5X－1, the recombinant expression vectors of BmKbpp, EGFP and BmKbpp／EGFP prokaryoticly fused with GST were constructed. These three expression vectors and pGEX－5X－1 were transformed into Rossetta(DE3) strains, respectively. Expression of BmKbpp gene in E. coli demonstrates that its product has antimicrobial function by testing the living curve of host cell. Although the fusing products of genes is toxic to host cell, the slight fusion expression of GST, BmKBPP and EGFP is successful, which provides us a way to obtain BmKBPP for further functional research.

Key words: scorpion toxins, antimicrobial peptides, BmKbpp, prokaryotic expression(责任编辑:陈　旷)