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. 1996 Feb 6;93(3):1221–1225. doi: 10.1073/pnas.93.3.1221

Structure-activity analysis of thanatin, a 21-residue inducible insect defense peptide with sequence homology to frog skin antimicrobial peptides.

P Fehlbaum 1, P Bulet 1, S Chernysh 1, J P Briand 1, J P Roussel 1, L Letellier 1, C Hetru 1, J A Hoffmann 1
PMCID: PMC40060  PMID: 8577744

Abstract

Immune challenge to the insect Podisus maculiventris induces synthesis of a 21-residue peptide with sequence homology to frog skin antimicrobial peptides of the brevinin family. The insect and frog peptides have in common a C-terminally located disulfide bridge delineating a cationic loop. The peptide is bactericidal and fungicidal, exhibiting the largest antimicrobial spectrum observed so far for an insect defense peptide. An all-D-enantiomer is nearly inactive against Gram-negative bacteria and some Gram-positive strains but is fully active against fungi and other Gram-positive bacteria, suggesting that more than one mechanism accounts for the antimicrobial activity of this peptide. Studies with truncated synthetic isoforms underline the role of the C-terminal loop and flanking residues for the activity of this molecule for which we propose the name thanatin.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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