Anthrax Research Today is a free monthly online journal that collates and summarizes the latest research about Anthrax, including details on bacillus anthracis, contagiousness, exposure, effects.

Stable peptide inhibitors prevent binding of lethal and oedema factors to protective antigen and neutralize anthrax toxin in vivo.

Pini A, Runci Y, Falciani C, Lelli B, Brunetti J, Pileri S, Fabbrini M, Lozzi L, Ricci C, Bernini A, Tonello F, Dal Molin F, Neri P, Niccolai N, Bracci L

Department of Molecular Biology, University of Siena, Via Fiorentina 1, 53100 Siena, Italy.

The lethal and oedema toxins produced by Bacillus anthracis, the aetiological agent of anthrax, are made by association of protective antigen with lethal and oedema factors and play a major role in the pathogenesis of anthrax. In the present paper, we describe the production of peptide-based specific inhibitors in branched form which inhibit the interaction of protective antigen with lethal and oedema factors and neutralize anthrax toxins in vitro and in vivo. Anti-protective antigen peptides were selected from a phage library by competitive panning with lethal factor. Selected 12-mer peptides were synthesized in tetra-branched form and were systematically modified to obtain peptides with higher affinity and inhibitory efficiency.

Published 10 March 2006 in Biochem J, 395(1): 157-63.
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