By P. Gopalakrishnakone (eds.)
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Additional resources for Biological Toxins and Bioterrorism: Biological Toxins and Bioterrorism
Example text
In summary, significant progress has been made in structural elucidation of the most poisonous biological toxin – the BoNTs and their mechanism of action. Novel inhibitors of protease activity of various BoNT serotypes have been identified. Developing these serotype-specific inhibitors into pan-active inhibitors remains a challenge and so does indication in animal models. Cross-References ▶ Bioactive Peptides Against Bioterror Agents ▶ Botulinum Neurotoxin Antidotes ▶ Botulinum Toxins: A review ▶ Counterfeit Botulinum Medical Products and Risk of Bioterrorism ▶ Diagnostics of Botulism References Adler M, Nicholson JD, Cornille F, Hackley Jr BE.
RIME complex from pdb id: 3D3X and NSC-77053 was docked using AutoDock program Fig. 8 Exosite inhibitors of BoNT/A and BoNT/B. In the upper panel, the BoNT/A catalytic domain is shown in complex with its substrate SNAP-25 (PDB id: 1XTG). BoNT/A is shown in surface representation; zinc is shown as a cyan sphere; and SNAP-25 is shown as a red ribbon (front and back views showing zinc-centered active site, the bexosite and the a-exosite). Lower panel shows the structures of the two natural-product inhibitors that bind at the exosites.
Novel inhibitors of protease activity of various BoNT serotypes have been identified. Developing these serotype-specific inhibitors into pan-active inhibitors remains a challenge and so does indication in animal models. Cross-References ▶ Bioactive Peptides Against Bioterror Agents ▶ Botulinum Neurotoxin Antidotes ▶ Botulinum Toxins: A review ▶ Counterfeit Botulinum Medical Products and Risk of Bioterrorism ▶ Diagnostics of Botulism References Adler M, Nicholson JD, Cornille F, Hackley Jr BE. Efficacy of a novel metalloprotease inhibitor on botulinum neurotoxin B activity.