Biological activities of cecropin B-thanatin hybrid peptides.
W Hongbiao, N Baolong, X Mengkui, H Lihua, S Weifeng, M Zhiqi
Index: J. Pept. Res. 66(6) , 382-6, (2005)
Full Text: HTML
Abstract
Ten kinds of hybrid peptides containing the N-terminal residues of cecropin B (CB) and C-terminal of thanatin (TH) were constructed and expressed as gluthathion S-transferase (GST)-fusion proteins. Variants were screened for the better biological activity, which was paralleled with the degree of growth inhibition of the transformant cells. The hybrid CB-TH g was selected as the best one among those hybrids by in vivo monitoring method and was chemical synthesized for in vitro antimicrobial activity analysis. The hybrid peptide showed rescued activity against several test strains when compared with the truncated isoforms of TH, suggesting that the peptides with different structure and mechanism could be used as templates for hybrid peptides design.
Related Compounds
Related Articles:
2011-02-01
[Appl. Environ. Microbiol. 77 , 1009-20, (2011)]
2012-10-01
[FEBS J. 279(20) , 3776-90, (2012)]
2013-06-01
[Colloids Surf. B Biointerfaces 110 , 225-35, (2013)]
A transgenic silkworm expressing the immune-inducible cecropin B-GFP reporter gene.
2006-05-01
[Insect Biochem. Mol. Biol. 36(5) , 429-34, (2006)]
Expression of the antimicrobial peptides in plants to control phytopathogenic bacteria and fungi.
2006-06-01
[Plant Cell Rep. 25(6) , 561-72, (2006)]