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

Infectious Diseases

Journal of AIDS & Clinical Research

Author(s): Fehlbaum P, Bulet P, Chernysh S, Briand JP, Roussel JP, , Fehlbaum P, Bulet P, Chernysh S, Briand JP, Roussel JP,

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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.
This article was published in Proc Natl Acad Sci U S A and referenced in Journal of AIDS & Clinical Research

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