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 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.
Cao
Yu
Y
Microbiology and Metabolic Engineering Key Laboratory of Sichuan Province, College of Life Sciences, Sichuan University, 610064 Sichuan, People's Republic of China.
Yu
Rong Qing
RQ
Liu
Yi
Y
Zhou
Huo Xiang
HX
Song
Ling Ling
LL
Cao
Yi
Y
Qiao
Dai Rong
DR
D000818:Animals; D000890:Anti-Infective Agents / Q000378:metabolism / Q000494:pharmacology*; D001419:Bacteria / Q000187:drug effects*; D054807:Cecropins / Q000235:genetics / Q000494:pharmacology* / Q000633:toxicity; D004912:Erythrocytes / Q000187:drug effects; D015870:Gene Expression; D006461:Hemolysis; D008555:Melitten / Q000235:genetics / Q000494:pharmacology* / Q000633:toxicity; D051379:Mice; D008826:Microbial Sensitivity Tests; D010843:Pichia / Q000235:genetics / Q000378:metabolism; D011993:Recombinant Fusion Proteins / Q000235:genetics / Q000494:pharmacology / Q000633:toxicity
D000890:Anti-Infective Agents; D054807:Cecropins; D011993:Recombinant Fusion Proteins; D008555:Melitten