61314-87-2

Upstream product

• 67-56-1 methanol 
• 76614-97-6 ammonium chloride salt of S-p-methoxybenzyl-(2R)-cysteine 
• 824-94-2 p-methoxybenzyl chloride 
• 2544-31-2 S-(4-methoxybenzyl)-L-cysteine 
• 77-76-9 2,2-dimethoxy-propane 
• 23619-36-5 Z(OMe)-Cys(MBzl)-OH 

Downstream Products

• 83176-23-2 N-tert-butyloxycarbonyl-S-(4-methoxybenzyl)cysteine methyl ester 
• 75946-61-1 Z(OMe)-Asn-Tyr-Cys(MBzl)-NHNH₂ 
• 78075-38-4 Z(OMe)-Asn-Tyr-Cys(MBzl)-OMe 

Relevant academic research and scientific papers

Bio-inspired nitrile hydration by peptidic ligands based on L-cysteine, L-methionine or L-penicillamine and pyridine-2,6-dicarboxylic acid

Nitrile hydratase (NHase, EC 4.2.1.84) is a metalloenzyme which catalyses the conversion of nitriles to amides. The high efficiency and broad substrate range of NHase have led to the successful application of this enzyme as a biocatalyst in the industrial syntheses of acrylamide and nicotinamide and in the bioremediation of nitrile waste. Crystal structures of both cobalt(III)- and iron(III)-dependent NHases reveal an unusual metal binding motif made up from six sequential amino acids and comprising two amide nitrogens from the peptide backbone and three cysteine-derived sulfur ligands, each at a different oxidation state (thiolate, sulfenate and sulfinate). Based on the active site geometry revealed by these crystal structures, we have designed a series of small-molecule ligands which integrate essential features of the NHase metal binding motif into a readily accessible peptide environment. We report the synthesis of ligands based on a pyridine-2,6-dicarboxylic acid scaffold and L-cysteine, L- S-methylcysteine, L-methionine or L-penicillamine. These ligands have been combined with cobalt(III) and iron(III) and tested as catalysts for biomimetic nitrile hydration. The highest levels of activity are observed with the L-penicillamine ligand which, in combination with cobalt(III), converts acetonitrile to acetamide at 1.25 turnovers and benzonitrile to benzamide at 1.20 turnovers.

GLUCOKINASE ACTIVATORS AND PHARMACEUTICAL COMPOSITIONS CONTAINING THE SAME AS AN ACTIVE INGREDIENT

The present invention relates to new compounds of formula (1) exhibiting excellent activity for glucokinase, and pharmaceutical compositions comprising the same as an active ingredient.

INDOLE COMPOUNDS AS AN INHIBITOR OF CELLULAR NECROSIS

The present invention relates to new indole compounds, pharmaceutically acceptable salts or isomers thereof which are useful for the prevention or treatment of cellular necrosis and necrosis-associated diseases. The present invention also relates to a method and a composition for the prevention or treatment of cellular necrosis and necrosis-associated diseases, comprising said indole compounds as an active ingredient.

GLUCOKINASE ACTIVATORS AND PHARMACEUTICAL COMPOSITIONS CONTAINING THE SAME AS AN ACTIVE INGREDIENT

The present invention relates to new compounds of formula (1) exhibiting excellent activity for glucokinase, and pharmaceutical compositions comprising the same as an active ingredient.

INDOLE COMPOUNDS AS AN INHIBITOR OF CELLULAR NECROSIS

The present invention relates to new indole compounds, pharmaceutically acceptable salts or isomers thereof which are useful for the prevention or treatment of cellular necrosis and necrosis-associated diseases. The present invention also relates to a method and a composition for the prevention or treatment of cellular necrosis and necrosis-associated diseases, comprising said indole compounds as an active ingredient.

Oxidative Deblocking of the 4-Methoxybenzyl Thioether Protecting Group: Application to the Directed Synthesis of Poly-cystinyl Peptides

The 4-methoxybenzyl thioether protecting group is deblocked efficiently by oxidation with the homogeneous electron transfer agent tris(4-bromophenyl)ammoniumyl (2.+) leading to the disulfide in high yields.S-(4-methoxybenzyl)cysteine derivatives like 9 in this way can be transformed into the corresponding cystine derivatives like 10 in 90percent yield.Many N and carboxy protecting groups like the Boc and Z group and tert-butyl or benzyl ester functions are stable under the cleavage conditions.On the other hand the 4-methoxybenzyl thioether protecting group is totally unaffected by the conditions for oxidative deblocking of the S-trityl functions by either iodine or rhodanolysis.This opens up new opportunities for the directed synthesis of cystinyl peptides with more than one intra- or interchain disulfide bridge.Application of the new method to the synthesis of a cystine peptide with one intrachain S-S-bridge and a double-chain biscystinyl peptide is reported.

Total Synthesis of Bovine Pancreatic Ribonuclease A. Part 5. Synthesis of the Protected S-Protein (Positions 21-124) and the Protected S-Peptide (Positions 1-20)

Starting from the protected tetraoctacontapeptide corresponding to the sequence Z(OMe)-(41-124)-OBzl of bovine pancreatic RNase, the protected S-protein Z(OMe)-(RNase 21-124)-OBzl was synthesized by six successive azide condensations of the peptide fragme