174464-16-5

Upstream product

• 5720-06-9 2-Methoxyphenylboronic acid 
• 34582-32-6 N-tert-butoxycarbonyl aspartic acid tert-butyl ester 
• 174464-14-3 α-tert-butyl N-(tertbutoxycarbonyl)-L-aspartate β-isoxazolidine 
• 31600-86-9 2-methoxyphenyllithium 

Downstream Products

• 174464-18-7 (S)-2-((tert-butoxycarbonyl)amino)-4-(2-methoxyphenyl)-4-oxobutanoic acid 
• 174464-21-2 Boc-An^oAsp-Ile-OCH₃ 
• 174464-25-6 BOC-Met-An^oAsp-Ile-OCH₃ 

Relevant academic research and scientific papers

Enantioselective synthesis of aroylalanine derivatives

In this paper we report the development of a highly enantioselective method for the synthesis of aroylalanines. The approach described employs a protected 2-amino-4-bromopent-4-enoic acid, generated via the asymmetric phase-transfer catalyzed alkylation of a glycine imine, as a key intermediate. Suzuki coupling with an aryl boronic acid followed by ozonolysis of the resulting styrene provides efficient access to the aroylalanine derivatives. The utility of this methodology is illustrated by the synthesis of L-kynurenine along with several aroylalanine inhibitors of the kynurenine pathway.

Palladium-Catalyzed Suzuki-Miyaura Reactions of Aspartic Acid Derived Phenyl Esters

Transition-metal-catalyzed transformations of amino acids and peptides could provide a powerful method for their site-selective modification. Here, we report non-decarbonylative Pd-catalyzed Suzuki-Miyaura reactions of phenyl ester derivatives of aspartic acid to form aryl-amino ketones. These products are potentially important in the synthesis of pharmaceuticals, and our methodology represents a new route to access molecules of this type.

Synthesis of anisolylated aspartyl and glutamyl tripeptides

A process has been developed for transforming the β-carboxyl of aspartate and the γ-carboxyl of glutamate into anisolyl ketones. These ketones are occasional byproducts in peptide synthesis, resulting from deprotection or resin-removal processes in the presence of anisole as a scavenger. The ketone amino acids have been incorporated in a tripeptide by coupling with CBMIT. During peptide bond formation the keto group of the glutamyl residue required protection, which was provided as the ethylene dithioketal.