1037516-58-7

Upstream product

• 100-09-4 4-methoxybenzoic acid 
• 7517-19-3 methyl (L)-leucinate hydrochloride 
• 100-07-2 4-methoxy-benzoyl chloride 
• 61-90-5 L-leucine 
• 67-56-1 methanol 
• 217446-37-2 4-iso-butyl-2-(4-methoxyphenyl)-5-oxo-4,5-dihydrooxazole 

Downstream Products

• 1403587-92-7 N-(1-(2-cyano-1,2-dimethylhydrazinyl)-4-methyl-1-oxopentan-2-yl)-4-methoxybenzamide 

Relevant academic research and scientific papers

Rational Design of 2-Substituted DMAP- N-oxides as Acyl Transfer Catalysts: Dynamic Kinetic Resolution of Azlactones

A novel concept that conversion of chiral 2-substituted DMAP into its DMAP-N-oxide could significantly enhance the catalytic activity and still be used as an acyl transfer catalyst is presented. A new type of chiral 2-substituted DMAP-N-oxides, derived from l-prolinamides, has been rationally designed, facilely synthesized, and applied in the dynamic kinetic resolution of azlactones. Using simple MeOH as the nucleophile, various l-amino acid derivatives were produced in high yields (up to 98% yield) and enantioselectivities (up to 96% ee). Furthermore, α-deuterium labeled l-phenylalanine derivative was also obtained. Experiments and DFT calculations revealed that in 2-substituted DMAP-N-oxide, the oxygen atom acted as the nucleophilic site and the N-H bond functioned as the H-bond donor. High enantioselectivity of the reaction was governed by steric factors, and the addition of benzoic acid reduced the activation energy by participating in the construction of a H-bond bridge. The theoretical chemical study indicated that only when attack directions of the chiral catalyst were fully considered could the correct calculation results be obtained. This work paves the way for the utilization of the C2 position of the pyridine ring and the development of chiral 2-substituted DMAP-N-oxides as efficient acyl transfer catalysts.

Highly selective azadipeptide nitrile inhibitors for cathepsin K: Design, synthesis and activity assays

We have developed a series of azadipeptide nitriles with different P3 groups. A triaryl meta-phenyl derivative, compound 13, was not only a potent inhibitor for cathepsin K (Ki = 0.0031 nM), but also highly selective over both cathepsins B and S (～1000-fold). A protein-ligand docking study performed on the series provided a possible explanation why compound 13 could be significantly more potent than the others, especially compound 12 in the same series.