206053-75-0

Upstream product

• 5292-43-3 bromoacetic acid tert-butyl ester 
• 2150-44-9 1-carbomethoxy-3,5-dihydroxybenzene 

Downstream Products

• 206053-76-1 3-[3-(tri-O-benzyl-α-L-fucopyranosyl)-1-propyloxy]-5-methoxycarbonylphenoxyacetic acid tert-butyl ester 
• 177735-50-1 (3-hydroxy-5-(methoxycarbonyl)phenoxy)acetic acid 
• 206053-92-1 {3-(2-Hydroxy-ethylcarbamoyl)-5-[3-((2S,3R,4R,5R,6S)-3,4,5-tris-benzyloxy-6-methyl-tetrahydro-pyran-2-yl)-propoxy]-phenoxy}-acetic acid 
• 206053-87-4 3-[3-(tri-O-benzyl-α-L-fucopyranosyl)-1-propyloxy]-5-methoxycarbonylphenoxyacetic acid 
• 787620-91-1 tert-butyl [5-({[3-({[(1R)-1-(4-fluorophenyl)ethyl]amino}carbonyl)-5-hydroxyphenoxy]acetyl}amino)pentyl]carbamate 
• 787620-90-0 methyl 3-[2-({5-[(tert-butoxycarbonyl)amino]pentyl}amino)-2-oxoethoxy]-5-hydroxybenzoate 

Relevant academic research and scientific papers

Identification of a small molecule nonpeptide active site β-secretase inhibitor that displays a nontraditional binding mode for aspartyl proteases

A small molecule nonpeptide inhibitor of β-secretase has been developed, and its binding has been defined through crystallographic determination of the enzyme-inhibitor complex. The molecule is shown to bind to the catalytic aspartate residues in an unprecedented manner in the field of aspartyl protease inhibition. Additionally, the complex reveals a heretofore unknown 83 subpocket that is created by the inhibitor. This structure has served an important role in the design of newer β-secretase inhibitors.

PHENYL CARBOXAMIDE COMPOUNDS USEFUL AS BETA-SECRETASE INHIBITORS FOR THE TREATMENT OF ALZHEIMER'S DISEASE

The present invention is directed to phenyl carboxamide compounds which are inhibitors of the beta-secretase enzyme and that are useful in the treatment of diseases in which the beta-secretase enzyme is involved, such as Alzheimer's disease. The invention is also directed to pharmaceutical compositions comprising these compounds and the use of these compounds and compositions in the treatment of such diseases in which the beta-secretase enzyme is involved.

Synthesis of novel Sialyl-Lewis(X) glycomimetics as selectin antagonists

A series of low molecular weight sialyl-Lewis(X) analogs based on either rigid or flexible replacements for the carbohydrates were designed as orally available anti-inflammatory drugs, synthesized and tested in cell-based adhesion assays. The flexible glycomimetic 7a lacking any glycoside or peptide linkage was prepared in 4 steps and 41% overall yield from methyl 3,5-dihydroxybenzoate and the fucose derivative 18 and exhibited about equal binding affinity to E- and P-selectin compared to the parent tetrasaccharide.