189030-32-8

Upstream product

• 2270-20-4 5-Phenylpentanoic acid 
• 150942-98-6 t-butyl lithioacetate 
• 540-88-5 acetic acid tert-butyl ester 
• 55628-85-8 1-Imidazol-1-yl-5-phenyl-pentan-1-one 

Downstream Products

• 235087-22-6 7-phenyl-3-trifluoromethanesulfonyloxy-hept-2-enoic acid tert-butyl ester 
• 209664-32-4 N-((R)-2-isobutyl-4-oxo-8-phenyl)octanoyl-3-(S)-amino-2-(R,S)-hydroxypentanoic acid ethyl amide 
• 209664-22-2 (R)-2-isobutyl-4-oxo-8-phenyloctanoic acid ((S)-1-hydroxymethyl-3-methyl)butyl amide 
• 209664-20-0 2-isobutyl-4-oxo-8-phenyloctanoic acid 
• 100848-88-2 6-Phenyl-1-hexyne 
• 209664-18-6 (R)-2-Isobutyl-4-oxo-8-phenyl-octanoic acid methyl ester 

Relevant academic research and scientific papers

Decarboxylative elimination of enol triflates as a general synthesis of acetylenes.

The enol trifluoromethanesulfonates 4, 8, 12, 17 and 20 of tert-butyl beta-ketodiesters and beta-ketoesters can be hydrolysed to the corresponding carboxylic acids by dissolution in trifluoroacetic acid. The dicarboxylic acids undergo mild decarboxylative elimination to give the acetylenic acids 4 and 9 in aqueous sodium bicarbonate solution at room temperature. Similarly, the monocarboxylic acids give the terminal and mid-chain acetylenes 13, 18, 21, and 24 by refluxing in acetone with potassium carbonate. One of the substituents on the acetylenes can be methyl, primary alkyl, secondary alkyl or ethynyl, and the other can be a carboxylic acid, hydrogen or primary alkyl, but the enol trifluoromethanesulfonates could not be prepared when one of the substituents was tert-butyl, nor when both substituents on the precursor to the acetylene were secondary alkyl.

Decarboxylative elimination of enol triflates as a general synthesis of acetylenes

Decarboxylative elimination of a range of enol triflates of β-keto esters gives acetylenes.

Exploration of the importance of the P2-P3-NHCO-moiety in a potent di- or tripeptide inhibitor of calpain I: insights into the development of nonpeptidic inhibitors of calpain I.

Calpain I, an intracellular cysteine protease, has been implicated in the neurodegeneration following an episode of cerebral ischemia. In this paper, we report on a series of peptidomimetic ketomethylene and carbamethylene inhibitors of recombinant human calpain I (rh calpain I). Our study reveals that the -NHCO-moiety (possible hydrogen-bonding site) at the P2-P3 region of a potent tripeptide or a dipeptide inhibitor of calpain I is not a strict requirement for enzyme recognition. Compounds 7d ((R)-2-isobutyl-4-oxo-4-(9-xanthenyl)butanoic acid ((S)-1-formyl-3-methyl)butyl amide), 31 ((R)-2-isobutyl-4-(2-sulfonylnaphthyl)butyric acid ((S)1-formyl-3-methyl)butyl amide) and 34 ((R)-2-isobutyl-4-(2-sulfoxylnaphthyl)butyric acid ((S)-1-formyl-3-methyl)butyl amide) which exhibited good activity in the enzyme assay, also inhibited calpain I in a human cell line.

Xanthene derived potent nonpeptidic inhibitors of recombinant human calpain I

Novel and potent, xanthene derived reversible aldehyde (7c) and α- ketocarboxamide (10a), and irreversible fluoromethyl ketone (10b) inhibitors of recombinant human calpain I are described.