95976-43-5

Basic information

• Product Name: Benzeneacetic acid, a-methyl-4-(1-methylethyl)-, (S)-
• Synonyms: (S)-2-(4-Isopropyl-phenyl)-propionic acid
• CAS NO: 95976-43-5
• Molecular Formula: C12H16O2
• Molecular Weight: 192.25400
• Mol File: 95976-43-5.mol
• Article Data: 2

Chemical Properties

• CAS DataBase Reference: Benzeneacetic acid, a-methyl-4-(1-methylethyl)-, (S)-(CAS DataBase Reference)
• NIST Chemistry Reference: Benzeneacetic acid, a-methyl-4-(1-methylethyl)-, (S)-(95976-43-5)
• EPA Substance Registry System: Benzeneacetic acid, a-methyl-4-(1-methylethyl)-, (S)-(95976-43-5)

Safety Data

• Hazardous Substances Data: 95976-43-5(Hazardous Substances Data)

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

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

Relevant articles and documents

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 The two C-terminal amino acids (EI) have been replaced by benzylamine derivatives and the pY + 1 glutamic acid has been substituted with leucine.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.