20432-29-5

Usage

InChI:InChI=1/C15H13NO/c16-15(17)14(13-9-5-2-6-10-13)11-12-7-3-1-4-8-12/h1-11H,(H2,16,17)/b14-11+

Upstream product

• 201230-82-2 carbon monoxide 
• 501-65-5 diphenyl acetylene 
• 91-47-4 (Z)-2,3-diphenylprop-2-enoic acid 
• 103593-12-0 trans-α-Phenyl-zimtsaeureimid 
• 91-48-5 (E)-2,3-diphenylpropenoic acid 
• 92-29-5 hydrobenzamide 
• 101-97-3 Ethyl 2-phenylethanoate 

Downstream Products

• 78956-21-5 (E)-α,β-Diphenylacrylsaeurethioamid 
• 87119-24-2 (2RS,3SR)-2,3-epoxy-2,3-diphenyl-propionic acid amide 

Relevant academic research and scientific papers

Palladium-Catalyzed Regioselective Hydroaminocarbonylation of Alkynes to α,β-Unsaturated Primary Amides with Ammonium Chloride

α,β-Unsaturated primary amides have found numerous applications in drug development, organic materials, and polymer sciences. However, the catalytic synthesis of α,β-unsaturated primary amides via carbonylation of alkynes has long been an elusive endeavor. Here, we report a novel palladium-catalyzed hydroaminocarbonylation of alkynes with NH4Cl as the amine source, enabling the highly chemo- and regioselective synthesis of α,β-unsaturated primary amides. A variety of alkynes, including aromatic alkynes, aliphatic alkynes, terminal alkynes, internal alkynes, as well as diynes with various functional groups, react well. The method turns the parasitic noncoordination ability of ammonium salts into a strategic advantage, enabling the gram-scale reaction to be performed in the presence of 0.05 mol % of catalyst with excellent selectivity.

Optimization and Evaluation of 5-Styryl-Oxathiazol-2-one Mycobacterium tuberculosis Proteasome Inhibitors as Potential Antitubercular Agents

This is the first report of 5-styryl-oxathiazol-2-ones as inhibitors of the Mycobacterium tuberculosis (Mtb) proteasome. As part of the study, the structure-activity relationship of oxathiazolones as Mtb proteasome inhibitors has been investigated. Furthermore, the prepared compounds displayed a good selectivity profile for Mtb compared to the human proteasome. The 5-styryl-oxathiazol-2-one inhibitors identified showed little activity against replicating Mtb, but were rapidly bactericidal against nonreplicating bacteria. (E)-5-(4-Chlorostyryl)-1,3,4-oxathiazol-2-one) was most effective, reducing the colony-forming units (CFU)/mL below the detection limit in only seven days at all concentrations tested. The results suggest that this new class of Mtb proteasome inhibitors has the potential to be further developed into novel antitubercular agents for synergistic combination therapies with existing drugs.