Biological activities of cecropin B-thanatin hybrid peptides.
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.
Hongbiao
W
W
Sericultural Institute, Zhejiang Academy of Agricultural Sciences, Hangzhou, China.
Baolong
N
N
Mengkui
X
X
Lihua
H
H
Weifeng
S
S
Zhiqi
M
M
D000595:Amino Acid Sequence; D000890:Anti-Infective Agents / Q000494:pharmacology*; D023181:Antimicrobial Cationic Peptides; D002678:Chimera / Q000235:genetics; D004926:Escherichia coli / Q000187:drug effects* / Q000235:genetics*; D019476:Insect Proteins / Q000494:pharmacology; D008826:Microbial Sensitivity Tests; D008969:Molecular Sequence Data; D010456:Peptides, Cyclic / Q000096:biosynthesis* / Q000494:pharmacology; D011993:Recombinant Fusion Proteins / Q000096:biosynthesis* / Q000302:isolation & purification / Q000494:pharmacology
D000890:Anti-Infective Agents; D023181:Antimicrobial Cationic Peptides; D019476:Insect Proteins; D010456:Peptides, Cyclic; D011993:Recombinant Fusion Proteins; C098076:thanatin; C031162:cecropin B protein, Insecta