447454-24-2

Upstream product

• 13807-89-1 2-(4-methoxybenzyloxy)ethanol 
• 124-63-0 methanesulfonyl chloride 
• 824-94-2 p-methoxybenzyl chloride 

Downstream Products

• 447454-26-4 5-(p-methoxybenzyloxy)-pentan-2-one 
• 1046818-86-3 [2-(R)-(cyclohexylhydroxyphenylmethyl)oxazol-5-ylmethyl]dimethyl-[2-(4-methoxybenzyloxy)ethyl]ammonium formate 
• 447454-25-3 1-((2-iodoethoxy)methyl)-4-methoxybenzene 

Relevant academic research and scientific papers

Generation of Alkoxyl Radicals by Photoredox Catalysis Enables Selective C(sp3)-H Functionalization under Mild Reaction Conditions

Reported herein is the first visible-light-induced formation of alkoxyl radicals from N-alkoxyphthalimides, and the Hantzsch ester as the reductant is crucial for the reaction. The selective hydrogen atom abstraction by the alkoxyl radical enables C(sp3)-H allylation and alkenylation reactions under mild reaction conditions at room temperature. Broad substrate variations, including a structurally complexed steroid, undergo the C(sp3)-H functionalization reaction effectively with high regio- and chemoselectivity.

SUBSTITUTED INDAZOLE DERIVATIVES ACTIVE AS KINASE INHIBITORS

The present invention relates to substituted indazole compounds which modulate the activity of protein kinases and are therefore useful in treating diseases caused by degulated protein kinase activity, like cancer. The present invention also provides methods for preparing these compounds, pharmaceutical compositions comprising these compounds, and methods of treating diseases utilizing such these compounds or the pharmaceutical compositions containing them.

OXAZOLE AND THIAZOLE DERIVATIVES AND THEIR USES

A quaternary ammonium compound of formula (I) having M3 receptor antagonist activity; a composition comprising such a compound; the use of such a compound in therapy (such as asthma or COPD); and a method of treating a patient with such a compound.

Photoaffinity analogues of farnesyl pyrophosphate transferable by protein farnesyl transferase

Farnesylation is a posttranslational lipid modification in which a 15-carbon farnesyl isoprenoid is linked via a thioether bond to specific cysteine residues of proteins in a reaction catalyzed by protein farnesyltransferase (FTase). We synthesized analogues (3-6) of farnesyl pyrophosphate (FPP) to probe the range of modifications possible to the FPP skeleton which allow for efficient transfer by FTase. Photoaffinity analogues of FPP (5, 6) were prepared by substituting perfluorophenyl azide functional groups for the ω-terminal isoprene of FPP. Substituted anilines replace the ω-terminal isoprene in analogues 3 and 4. Compounds 3-5 were prepared by reductive amination of the appropriate anilines with 8-oxogeranyl acetate, followed by ester hydrolysis, chlorination, and pyrophosphorylation. Additional substitution of three methylenes for the β-isoprene of FPP gave photoprobe 6 in nine steps. Preparation of the analogues required TiCl4-mediated imine formation prior to NaBH(OAc)3 reduction for anilines with a pKa 3PCl2 conversion of allylic alcohols 13-16 into corresponding chlorides 17-20. Analogues 3-6 are efficiently transferred to target N- dansyl-GCVLS peptide substrate by mammalian FTase. Comparison of analogue structures and kinetics of transfer to those of FPP reveals that ring fluorination and para substituents have little effect on the affinity of the analogue pyrophosphate for FTase and its transfer efficiency. These results are also supported with models of the analogue binding modes in the active site of FTase. The transferable azide photoprobe 5 photoinactivates FTase. Transferable analogues 5 and 6 allow the formation of appropriately posttranslationally modified photoreactive peptide probes of isoprene function.