STRUCTURE-ACTIVITY ANALYSIS OF THANATIN, A 21-RESIDUE INDUCIBLE INSECT DEFENSE PEPTIDE WITH SEQUENCE HOMOLOGY TO FROG-SKIN ANTIMICROBIAL PEPTIDES

Citation
P. Fehlbaum et al., STRUCTURE-ACTIVITY ANALYSIS OF THANATIN, A 21-RESIDUE INDUCIBLE INSECT DEFENSE PEPTIDE WITH SEQUENCE HOMOLOGY TO FROG-SKIN ANTIMICROBIAL PEPTIDES, Proceedings of the National Academy of Sciences of the United Statesof America, 93(3), 1996, pp. 1221-1225
Citations number
20
Language
INGLESE
art.tipo
Article
Categorie Soggetti
Multidisciplinary Sciences
ISSN journal
0027-8424
Volume
93
Issue
3
Year of publication
1996
Pages
1221 - 1225
Database
ISI
SICI code
0027-8424(1996)93:3<1221:SAOTA2>2.0.ZU;2-6
Abstract
Immune challenge to the insect Podisus maculiventris induces synthesis of a 21-residue peptide with sequence homology to Frog skin antimicro bial peptides of the brevinin family, The insect and frog peptides hav e in common a C-terminally located disulfide bridge delineating a cati onic loop, The peptide is bactericidal and fungicidal, exhibiting the largest antimicrobial spectrum observed so far for an insect defense p eptide, An all-D-enantiomer is nearly inactive against Gram-negative b acteria and some Gram-positive strains but is fully active against fun gi and other Gram-positive bacteria, suggesting that more than one mec hanism accounts for the antimicrobial activity of this peptide, Studie s with truncated synthetic isoforms underline the role of the C-termin al loop and flanking residues for the activity of this molecule for wh ich we propose the name thanatin.