94062-52-9

Usage

InChI:InChI=1/C16H21NO2.C7H8O3S/c18-16(19-11-12-6-2-1-3-7-12)15-10-13-8-4-5-9-14(13)17-15;1-6-2-4-7(5-3-6)11(8,9)10/h1-3,6-7,13-15,17H,4-5,8-11H2;2-5H,1H3,(H,8,9,10)

Upstream product

• 80875-98-5 (2S,3aS,7aS)-perhydroindole-2-carboxylic acid 
• 104-15-4 toluene-4-sulfonic acid 
• 100-51-6 benzyl alcohol 
• 79815-20-6 (S)-indoline-2-carboxylic acid 

Downstream Products

• 122454-52-8 (2S,3aS,7aS)-1-[(2S)-2-[[(1S)-1-(ethoxycarbonyl)butyl]amino]-1-oxopropyl]octahydro-1H-indole-2-carboxylic acid benzyl ester 
• 671203-92-2 Benzyl (2S,3aS,7aS)-1-{(2S)-2-[(tert-butyloxycarbonyl)-amino]-propionyl}-octahydro-1H-indole-2-carboxylate 
• 64407-57-4 N,N-dicyclohexylurea 
• 130933-21-0 (2S,3aS,7aS)-1-glycinyl>-2-carboxyperhydroindole tert-butylamine salt 
• 130933-17-4 (2S,3aS,7aS)-1-glycinyl>-2-carboxyperhydroindole 
• 130933-19-6 (2S,3aS,7aS)-1-glycinyl>-2-<(benzyloxy)carbonyl>perhydroindole 

Relevant academic research and scientific papers

Novel method for synthesissing (2s,3as,7as)-perhydroindole-2-carboxylic acid and the esters thereof and the use thereof for perindopril synthesis

Process for the synthesis of compounds of formula (I): wherein R represents hydrogen or a protecting group. Application in the synthesis of perindopril and pharmaceutically acceptable salts thereof.

Configuration and preferential solid-state conformations of perindoprilat (S-9780). Comparison with the crystal structures of other ACE inhibitors and conclusions related to structure-activity relationships

The conformation of perindoprilat, an antihypertensive drug, is studied in the solid state by X-ray analysis. The resolution of its structure reveals important analogies between its observed conformation and that of several ACE inhibitors of the same family. This comparison points out a constant relative orientation of the functional groups, regardless of the molecular environment. This angular constancy appears to us as not being accidental and is a good argument for the spatial design of the ACE binding site. Although ACE is a carboxydipeptidase, the binding site may not contain two but one unique hydrophobic pocket receiving the C-terminal end of the inhibitors.