433219-87-5

Upstream product

• 114672-02-5 1-benzylcyclobutane-1-carboxylic acid 
• 114672-01-4 ethyl 1-benzylcyclobutane-1-carboxylate 
• 14924-53-9 ethyl cyclobutylcarboxylate 
• 100-39-0 benzyl bromide 
• 3721-95-7 Cyclobutanecarboxylic acid 
• 620-05-3 iodomethylbenzene 

Downstream Products

• 568591-06-0 {(S)-1-[Hydroxy-((R)-1-phenyl-ethylcarbamoyl)-methyl]-pentyl}-carbamic acid 1-benzyl-cyclobutylmethyl ester 
• 433220-28-1 (Z)-7-[(1R,2R,3R)-2-[(E)-4-(1-Benzyl-cyclobutyl)-4-(tert-butyl-dimethyl-silanyloxy)-but-1-enyl]-3-(tert-butyl-dimethyl-silanyloxy)-5-oxo-cyclopentyl]-hept-5-enoic acid methyl ester 
• 212310-02-6 (Z)-7-{(1R,2R,3R)-2-[(E)-(R)-4-(1-Benzyl-cyclobutyl)-4-hydroxy-but-1-enyl]-3-hydroxy-5-oxo-cyclopentyl}-hept-5-enoic acid methyl ester 
• 433220-13-4 (E)-1-iodo-4-(tert-butyldimethylsiloxy)-6-phenyl-5,5-trimethylene-1-hexene 
• 433220-00-9 [1-(1-benzyl-cyclobutyl)-but-3-ynyloxy]-tert-butyl-dimethyl-silane 

Relevant academic research and scientific papers

Potent and selective P2-P3 ketoamide inhibitors of cathepsin K with good pharmacokinetic properties via favorable P 1′, P1, and/or P3 substitutions

A series of ketoamides were synthesized and evaluated for inhibitory activity against cathepsin K. Exploration of the interactions between achiral P2 substituents and the cysteine protease based on molecular modeling suggestions resulted in potent cathepsin K inhibitors that demonstrated high selectivity versus cathepsins B, H, and L. Subsequent modifications of the P3, P1, and P1′ moieties afforded orally bioavailable inhibitors. A series of ketoamides were synthesized and evaluated for inhibitory activity against cathepsin K. Exploration of the interactions between achiral P2 substituents and the cysteine protease based on molecular modelling suggestions resulted in potent cathepsin K inhibitors that demonstrated high selectivity versus cathepsins B, H, and L. Subsequent modifications of the P3, P1, and P1′ moieties afforded orally bioavailable inhibitors.

Development of a highly selective EP2-receptor agonist. Part 1: Identification of 16-hydroxy-17,17-trimethylene PGE2 derivatives

Design and synthesis of an EP2-receptor selective agonist began with the chemical modification of α and ω-chains of butaprost 1a, which exhibits an affinity for the IP-receptor. Two series of prostaglandin (PG) analogues with a 16-hydroxy-17,17-trimethylene moiety as an ω-chain were identified. Among those tested, 4a,b,e,f,h and 6a,b,e,f,h were found to be highly selective EP2-receptor agonists. Structure activity relationships are discussed. Copyright