95976-43-5

Upstream product

• 52629-44-4 4-(1-methylethyl)-benzeneacetyl chloride 
• 222737-10-2 (S)-4-Isopropyl-3-[(S)-2-(4-isopropyl-phenyl)-propionyl]-oxazolidin-2-one 
• 58929-93-4 Ethyl 2-(4-isopropylphenyl)propanoate 

Downstream Products

• 222737-11-3 [(S)-1-(4-Isopropyl-phenyl)-ethyl]-carbamic acid benzyl ester 
• 68285-22-3 (S)-1-(4-isopropylphenyl)ethylamine 
• 222737-09-9 Phosphoric acid mono-[4-((S)-2-acetylamino-2-{(S)-1-[(S)-1-(4-isopropyl-phenyl)-ethylcarbamoyl]-3-methyl-butylcarbamoyl}-ethyl)-phenyl] ester 

Relevant academic research and scientific papers

Phosphotyrosine-containing dipeptides as high-affinity ligands for the p56(lck) SH2 domain

Src homology-2 (SH2) domains are noncatalytic motifs containing approximately 100 amino acid residues that are involved in intracellular signal transduction. The phosphotyrosine-containing tetrapeptide Ac-pYEEI binds to the SH2 domain of p56(lck) (Lck) with an affinity of 0.1 μM. Starting from Ac-pYEEI, we have designed potent antagonists of the Lck SH2 domain which are reduced in peptidic character and in which the three carboxyl groups have been eliminated. The two C-terminal amino acids (EI) have been replaced by benzylamine derivatives and the pY + 1 glutamic acid has been substituted with leucine. The best C-terminal fragment identified, (S)-1-(4-isopropylphenyl)ethylamine, binds to the Lck SH2 domain better than the C-terminal dipeptide EI. Molecular modeling suggests that the substituents at the 4-position of the phenyl ring occupy the pY + 3 lipophilic pocket in the SH2 domain originally occupied by the isoleucine side chain. This new series of phosphotyrosine-containing dipeptides binds to the Lck SH2 domain with potencies comparable to that of tetrapeptide 1.

Chemoenzymatic synthesis of pure enantiomeric 2-aryl propionic acids

A new chemoenzymatic procedure to obtain pure enantiomeric 2-arylpropionic acids is described. The one pot synthesis of (±)-2-arylpropionic acids is carried out by addition of dichlorocarbene to the C=O bond of arylmethylketones and hydrogenolysis of the additon product. The racemic mixture is resolved by enantiospecific hydrolysis of the racemic ethyl esters using native lipase from Candida rugosa. The good yields, the accessibility of the starting arylmethylketones and the stereospecificity of the enzymatic hydrolysis make the process interesting in order to obtain the same non steroidal antiinflammatory drugs such as Ibuprofen or Naproxen.