403503-40-2

Upstream product

• 64-18-6 formic acid 
• 403503-37-7 (2S,4R)-1-benzyl 2-methyl 4-hydroxypiperidine-1,2-dicarboxylate 
• 475504-28-0 4-formyloxy-(S)-pipecolic acid methyl ester 
• 85-44-9 phthalic anhydride 
• 211058-80-9 methyl 4(R)-hydroxypiperidine-2(S)-carboxylate 
• 403503-26-4 (2S,4R)-4-Hydroxy-1-((S)-1-phenyl-ethyl)-piperidine-2-carboxylic acid methyl ester 
• 501-53-1 benzyl chloroformate 

Downstream Products

• 211055-73-1 (2S,4R)-4-(2,4-Dichloro-phenoxy)-piperidine-2-carboxylic acid methyl ester 
• 403503-55-9 (2S,4R)-4-Fluoro-piperidine-1,2-dicarboxylic acid 1-benzyl ester 2-methyl ester 
• 403503-52-6 cis-4-fluoro-(S)-pipecolic acid 
• 403503-43-5 methyl 1-benzyloxycarbonyl-trans-4-hydroxy-(S)-pipecolate 

Relevant academic research and scientific papers

Chemoenzymatic synthesis of the four diastereoisomers of 4-hydroxypipecolic acid from N-acetyl-(R,S)-allylglycine: Chiral scaffolds for drug discovery

All four diastereoisomers of 4-hydroxypipecolic acid were prepared in a form conveniently protected for drug discovery applications with the use of industrially scaleable methodology. Resolution of the racemic starting material using proprietary acylases followed by an acyliminium ion cyclisation gave diastereomeric mixtures of 4-formyloxypipecolic acid, which were differentiated using an enzyme-catalysed hydrolysis. The products were separated by partition, and by following a sequence of straightforward chemical steps, the individual stereoisomers of the protected 4-hydroxypipecolates were crystallized to optical purity in 100 g quantities.

Stereoselective syntheses of 4-fluoro- and 4,4-difluoropipecolic acids

Stereoselective syntheses of 4-fluoro- and 4,4-difluoropipecolic acids starting from Z-protected 4-hydroxy- and 4-oxopipecolates via fluorodehydroxylation and fluorodeoxygenation are described.

Novel constrained CCK-B dipeptoid antagonists derived from pipecolic acid

A new series of 4-substituted pipecolic acid derivatives was prepared and incorporated into dipeptoids. The resulting products behave as moderately potent CCK-B antagonists but their constrained structure and its comparison with structurally related compounds yield valuable information about the conformational requirements for optimal recognition of the CCK-B receptor by antagonists.