67853-00-3

Upstream product

• 106262-52-6 10-undecenoic acid benzyl ester 
• 1679-53-4 10-hydroxydecanoic acid 
• 100-39-0 benzyl bromide 

Downstream Products

• 329309-18-4 benzyl 10-oxodecanoate 
• 329309-24-2 benzyl N,N',N''-tris(tert-butoxycarbonyl)-N-{N'-[N''-(2-{tert-butyldimethylsilyloxy}ethyl)-10-aminodecanoyloxyethyl]-10-aminodecanoyloxyethyl}-10-aminodecanoate 
• 329309-25-3 benzyl N,N',N''-tris(tert-butoxycarbonyl)-N-{N'-[N''-(2-hydroxyethyl)-10-aminodecanoyloxyethyl]-10-aminodecanoyloxyethyl}-10-aminodecanoate 
• 329309-22-0 benzyl N,N'-bis(tert-butoxycarbonyl)-N-{N'-[2-(tert-butyldimethylsilyloxy)ethyl]-10-aminodecanoyloxyethyl}-10-aminodecanoate 
• 329309-23-1 benzyl N,N'-bis(tert-butoxycarbonyl)-N-[N'-(2-hydroxyethyl)-10-aminodecanoyloxyethyl]-10-aminodecanoate 
• 329309-20-8 benzyl N-(tert-butoxycarbonyl)-N-[2-(tert-butyldimethylsilyloxy)ethyl]-10-aminodecanoate 
• 329309-19-5 benzyl N-(tert-butoxycarbonyl)-N-(2-hydroxyethyl)-10-aminodecanoate 

Relevant academic research and scientific papers

Design, synthesis, and kinetic evaluation of high-affinity FKBP ligands and the X-ray crystal structures of their complexes with FKBP 12

The design and synthesis of high-affinity FKBP12 ligands is described. These compounds potently inhibit the cis-trans-peptidylprolyl isomerase (rotamase) activity catalyzed by FKBP12 with inhibition constants (Ki,app) as low as 1 nM, yet they possess remarkable structural simplicity relative to FK506 and rapamycin, from which they are conceptually derived. The atomic structures of three FKBP12-ligand complexes and of one unbound ligand were determined by X-ray crystallography and are compared to the FKBP12-FK506 and FKBP12-rapamycin complexes.