Structure-activity analysis of thanatin, a 21-residue inducible insect defense peptide with sequence homology to frog skin antimicrobial peptides
P Fehlbaum, P Bulet, S Chernysh… - Proceedings of the …, 1996 - National Acad Sciences
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
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
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