945405-33-4

Upstream product

• 945405-59-4 C₂₃H₃₅NO₅Si 
• 332882-89-0 1-amino-4-[N²,N³-bis(tert-butoxycarbonyl)guanidino]butane 
• 69739-34-0 t-butyldimethylsiyl triflate 
• 332882-89-0 4-[2,3-bis(tert-butoxycarbonyl)guanidino]butylamine 
• 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 
• 320748-69-4 (2S,3aS,6R,7aS)-6-hydroxy-2,3,3a,4,5,6,7,7a-octahydroindole-1,2-dicarboxylic acid 1-benzyl ester 2-methyl ester 

Downstream Products

• 945405-61-8 C₄₇H₇₉ClN₆O₁₀Si 

Relevant academic research and scientific papers

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.