864801-48-9

Upstream product

• 6638-79-5 N,O-dimethylhydroxylamine*hydrochloride 
• 109183-71-3 N-(tert-butoxycarbonyl)-L-cyclohexylglycine 

Downstream Products

• 1337862-59-5 (S)-tert-butyl 1-cyclohexyl-2-oxopent-4-enylcarbamate 
• 1337862-67-5 tert-butyl (1S,2R)-2-(tert-butyldimethylsilyloxy)-1-cyclohexylpent-4-enylcarbamate 
• 1337862-61-9 tert-butyl (1S,2R)-1-cyclohexyl-2-hydroxypent-4-enylcarbamate 
• 1337862-74-4 (2S,3R)-tert-butyl 3-(tert-butyldimethylsilyloxy)-2-cyclohexyl-5-oxopyrrolidine-1-carboxylate 
• 881902-40-5 (4S,5S)-5-({(S)-1-[2-({[((S)-tert-Butoxycarbonyl-phenyl-methyl)-carbamoyl]-methyl}-carbamoyl)-1-cyclopropylmethyl-2-oxo-ethylcarbamoyl]-2-cyclopropyl-ethylcarbamoyl}-methyl)-4-cyclohexyl-2,2-dimethyl-oxazolidine-3-carboxylic acid isobutyl ester 
• 905927-66-4 5-({1-[2-({[(tert-butoxycarbonyl-phenyl-methyl)-carbamoyl]-methyl}-carbamoyl)-1-cyclopropylmethyl-2-hydroxy-ethylcarbamoyl]-2-cyclopropyl-ethylcarbamoyl}-methyl)-4-cyclohexyl-2,2-dimethyl-oxazolidine-3-carboxylic acid isobutyl ester 
• 881902-35-8 (4S,5S)-5-Carboxymethyl-4-cyclohexyl-2,2-dimethyl-oxazolidine-3-carboxylic acid isobutyl ester 

Relevant academic research and scientific papers

Structure-Based Design of Inhibitors Selective for Human Proteasome β2c or β2i Subunits

Subunit-selective proteasome inhibitors are valuable tools to assess the biological and medicinal relevance of individual proteasome active sites. Whereas the inhibitors for the β1c, β1i, β5c, and β5i subunits exploit the differences in the substrate-binding channels identified by X-ray crystallography, compounds selectively targeting β2c or β2i could not yet be rationally designed because of the high structural similarity of these two subunits. Here, we report the development, chemical synthesis, and biological screening of a compound library that led to the identification of the β2c- and β2i-selective compounds LU-002c (4; IC50 β2c: 8 nM, IC50 β2i/β2c: 40-fold) and LU-002i (5; IC50 β2i: 220 nM, IC50 β2c/β2i: 45-fold), respectively. Co-crystal structures with β2 humanized yeast proteasomes visualize protein-ligand interactions crucial for subunit specificity. Altogether, organic syntheses, activity-based protein profiling, yeast mutagenesis, and structural biology allowed us to decipher significant differences of β2 substrate-binding channels and to complete the set of subunit-selective proteasome inhibitors.

Depeptidization efforts on P3-P′2 α-ketoamide inhibitors of HCV NS3-4A serine protease: Effect on HCV replicon activity

Depeptidization efforts of the P3-P2 region of P 3 capped α-ketoamide inhibitor of HCV NS3 serine protease 1 are reported. We clearly established that N-methylation of the P2 nitrogen and modification of the P2′