Metallopeptidase inhibitors of tetanus toxin: A combinatorial approach.

@article{Martin1999MetallopeptidaseIO,
  title={Metallopeptidase inhibitors of tetanus toxin: A combinatorial approach.},
  author={Lo{\"i}c Martin and F. Cornille and Serge Turcaud and Herv{\'e} Meudal and B. Roques and Marie-Claude Fourni{\'e}-Zaluski},
  journal={Journal of medicinal chemistry},
  year={1999},
  volume={42 3},
  pages={515-25}
}
The bacterial protein tetanus toxin (TeNt), which belongs to the family of zinc endopeptidases, cleaves synaptobrevin, an essential synaptic protein component of the neurotransmitter exocytosis apparatus, at a single peptide bond (Gln76-Phe77). This protease activity is a particularly attractive target for designing potent and selective synthetic inhibitors as a possible drug therapy for tetanus. beta-Aminothiols mimicking Gln76 of synaptobrevin have been previously shown to inhibit the tetanus… CONTINUE READING