213488-17-6

Basic information

• Product Name: Thioacetic acid S-[(S)-2-tert-butoxycarbonylamino-4-(trityl-carbamoyl)-butyl] ester
• Synonyms: Thioacetic acid S-[(S)-2-tert-butoxycarbonylamino-4-(trityl-carbamoyl)-butyl] ester
• CAS NO: 213488-17-6
• Molecular Weight: 532.704
• Mol File: 213488-17-6.mol
• Article Data: 1

Chemical Properties

• CAS DataBase Reference: Thioacetic acid S-[(S)-2-tert-butoxycarbonylamino-4-(trityl-carbamoyl)-butyl] ester(CAS DataBase Reference)
• NIST Chemistry Reference: Thioacetic acid S-[(S)-2-tert-butoxycarbonylamino-4-(trityl-carbamoyl)-butyl] ester(213488-17-6)
• EPA Substance Registry System: Thioacetic acid S-[(S)-2-tert-butoxycarbonylamino-4-(trityl-carbamoyl)-butyl] ester(213488-17-6)

Safety Data

• Hazardous Substances Data: 213488-17-6(Hazardous Substances Data)

Upstream product

• 507-09-5 tiolacetic acid 
• 213488-16-5 [(S)-1-Hydroxymethyl-3-(trityl-carbamoyl)-propyl]-carbamic acid tert-butyl ester 
• 132388-69-3 Boc-L-Gln(Trt)-OH 

Downstream Products

• 213487-85-5 (S)-4-Amino-5-[(S)-2-amino-4-(trityl-carbamoyl)-butyldisulfanyl]-pentanoic acid trityl-amide 
• 213488-18-7 [(S)-1-[(S)-2-tert-Butoxycarbonylamino-4-(trityl-carbamoyl)-butyldisulfanylmethyl]-3-(trityl-carbamoyl)-propyl]-carbamic acid tert-butyl ester 

Relevant articles and documents

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.