213487-97-9

Upstream product

• 213487-96-8 3-(tert-Butoxycarbonylamino-ethoxycarbonyl-methyl)-benzoic acid ethyl ester 
• 2196-57-8 amino-(3-carboxy-phenyl)-acetic acid 

Downstream Products

• 213488-22-3 Thioacetic acid S-[2-tert-butoxycarbonylamino-2-(3-dimethylcarbamoyl-phenyl)-ethyl] ester 
• 213487-99-1 Thioacetic acid S-[2-tert-butoxycarbonylamino-2-(3-carbamoyl-phenyl)-ethyl] ester 
• 213488-21-2 [1-(3-Dimethylcarbamoyl-phenyl)-2-hydroxy-ethyl]-carbamic acid tert-butyl ester 
• 213487-98-0 [1-(3-Carbamoyl-phenyl)-2-hydroxy-ethyl]-carbamic acid tert-butyl ester 

Relevant academic research and scientific papers

β-Amino-thiols inhibit the zinc metallopeptidase activity of tetanus toxin light chain

Tetanus neurotoxin is a 150-kDa protein produced by Clostridium tetani, which causes the lethal spastic paralytic syndromes of tetanus by blocking inhibitory neurotransmitter release at central synapses. The toxin light chain (50 kDa) has a zinc endopeptidase activity specific for synaptobrevin, an essential component of the neuroexocytosis apparatus. Previous unsuccessful attempts to block the proteolytic activity of this neurotoxin with well-known inhibitors of other zinc proteases led us to study the design of specific inhibitors as a possible drug therapy to prevent the progressive evolution of tetanus following infection. Starting from the synaptobrevin sequence at the level of the cleavage site by tetanus neurotoxin (Gln76- Phe77)a thiol analogue of glutamine demonstrated inhibitory activities in the millimolar range. A structure-activity relationship performed with this compound led us to determine the requirement for the correct positioning of the thiol group, the primary amino group, and a carboxamide or sulfonamide group on the side chain. This resulted in the design of a β-amino(4- sulfamoylphenyl)glycine-thiol, the first significantly efficient inhibitor of tetanus neurotoxin with a K(i) value of 35 ± 5μM.