320748-69-4

Upstream product

• 171523-63-0 <2S-(2β,3aβ,7aβ)>-2,3,3a,6,7,7a-hexahydro-3a-benzoyloxy-6-oxo-1H-indole-1,2-dicarboxylic acid 1-benzyl 2-methyl ester 
• 144534-49-6 (2S,3aR,7aR)-3a-hydroxy-6-oxo-2,3,3a,6,7,7a-hexahydroindole-1,2-dicarboxylic acid 1-benzyl ester 2-methyl ester 
• 320748-67-2 (2S,3aS,7aS)-6-oxo-2,3,3a,4,5,6,7,7a-octahydroindole-1,2-dicarboxylic acid 1-benzyl ester 2-methyl ester 
• 320748-68-3 1-benzyl 2-methyl (2S,3aS,6S,7aS)-6-hydroxyoctahydro-1H-indole-1,2-dicarboxylate 
• 320748-65-0 (2S,3aS,7aS)-3a-(benzoyloxy)-6-oxo-2,3,3a,6,7,7a-hexahydroindole-1,2-dicarboxylic acid 1-benzyl ester 2-methyl ester 
• 320748-66-1 (2S,7aS)-6-oxo-2,3,5,6,7,7a-hexahydroindole-1,2-dicarboxylic acid 1-benzyl ester 2-methyl ester 

Downstream Products

• 320748-70-7 (2S,3aS,6R,7aS)-6-(tert-butyldimethylsiloxy)-2,3,3a,4,5,6,7,7a-octahydroindole-1,2-dicarboxylic acid 1-benzyl ester 2-methyl ester 
• 945405-32-3 C₂₀H₂₇NO₆ 
• 320748-85-4 C₄₇H₇₃N₅O₉Si₂ 
• 320748-86-5 C₇₃H₁₂₂N₆O₁₁Si₄ 
• 320748-89-8 C₇₃H₁₂₂N₆O₁₁Si₄ 
• 945405-63-0 C₂₈H₄₂N₂O₈ 

Relevant academic research and scientific papers

Investigating the Toxicity of the Aeruginosin Chlorosulfopeptides by Chemical Synthesis

Harmful algal blooms are becoming more prevalent all over the world, and identification and mechanism-of-action studies of the responsible toxins serve to protect ecosystems, livestock, and humans alike. In this study, the chlorosulfopeptide aeruginosin 8

Total synthesis and structural revision of the presumed aeruginosins 205A and B

A stereoselective synthesis of enantiopure aeruginosin 205B aglycon confirms the presence of a (3R,2S)-3-chloroleucine amide residue and a (6R)-hydroxy (4aR,7aS)-octahydroindole-(2S)-2-carboxamide (Choi) subunit instead of a 6-chloro-substituted core (Cco

Structure-based organic synthesis of unnatural aeruginosin hybrids as potent inhibitors of thrombin

Based on X-ray crystallographic data of complexes of chlorodysinosin A with the enzyme thrombin, a series of analogs were synthesized varying the nature of the P1, P2, and P3 pharmacophoric sites and the central octahydroindole carboxyamide core. In general, introduction of a hydrophobic substituent on the d-leucine amide residue dramatically improved the inhibition of the enzyme. This is rationalized based on a better fit of the P3 subunit in the hydrophobic S3 enzyme site. Single digit nanomolar inhibition expressed as IC50 was observed for several analogs.

Total synthesis and stereochemical revision of (+)-aeruginosin 298-A.

[structure:see text] Novel routes toward both enantiomers of the bicyclic proline surrogate 2-carboxy-6-hydroxyoctahydroindole, i.e., Choi, were developed on the basis of the oxidative cyclization of L-tyrosine. Synthesis of the proposed sequence of (+)-a