69222-99-7

Upstream product

• 462-10-2 DL-homocystine 
• 501-53-1 benzyl chloroformate 

Downstream Products

• 1452406-84-6 (Cbz-D,L-Homo-Cys-Bt)₂ 
• 1452406-90-4 (Cbz-D,L-Homo-Cys-D-Pro-Bt)₂ 
• 1452406-87-9 (Cbz-D,L-Homo-Cys-D-Pro-OH)₂ 
• 1452406-93-7 bis[cyclo-(Cbz-D,L-Homo-Cys-D-Pro)] 
• 213487-91-3 Dimethyl (2RS,2'RS)-N,N'-bis(benzyloxycarbonyl)homocysteinate 
• 69164-70-1 2-Benzyloxycarbonylamino-4-(3-benzyloxycarbonyl-3-benzyloxycarbonylamino-propyldisulfanyl)-butyric acid benzyl 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.

Potential antitumor agents via inhibitors of L-asparagine synthetase: substituted sulfonamides and sulfonyl hydrazides related to glutamine

A series of 4-(substituted aminosulfonyl)- and 4-(substituted hydrazinosulfonyl)-2-aminobutanoic acids, compounds structurally related to glutamine, was synthesized as potential inhibitors of L-asparagine synthetase and subjected to screening as antitumor agents. Target amino acids were obtained by condensation of a blocked reactive sulfonyl chloride with the appropriate amine or hydrazide, followed by deblocking with hydrogen-palladium or liquid hydrogen fluoride-anisole. Neither the target compounds nor their protected precursors inhibited the enzyme from L5178Y/AR or prolonged the life of mice with P-388 lymphocytic leukemia. However, DL-4,4'-dithiobis[2-(benzyloxycarbonylamino)-butanoic acid], an intermediate in the synthesis of the target amino acids, exhibited 90% inhibition of L-asparagine synthetase at 10 mM.