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Design, Recombinant Expression, and Antibacterial Activity of the Cecropins–Melittin Hybrid Antimicrobial Peptides

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 p...

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Bibliographic Details
Published in:Current microbiology 2010-09, Vol.61 (3), p.169-175
Main Authors: Cao, Yu, Yu, Rong Qing, Liu, Yi, Zhou, Huo Xiang, Song, Ling Ling, Cao, Yi, Qiao, Dai Rong
Format: Article
Language:English
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Summary: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.
ISSN:0343-8651
1432-0991
DOI:10.1007/s00284-010-9592-7