6719-79-5

Upstream product

• 770-12-7 O-phenyl phosphorodichloridate 
• 108-95-2 phenol 
• 677-24-7 methyl dichlorophosphoridate 
• 67-56-1 methanol 

Downstream Products

• 59045-84-0 C₁₁H₁₀NO₃P 
• 68729-27-1 C₁₂H₁₂NO₃P 
• 83472-82-6 N-phenylphosphoryl-4-N',N'-dimethylaminopyridinium 
• 4009-39-6 methyl phenyl hydrogen phosphate 
• 1432474-88-8 (E)-ethyl 3-(2-((dimethoxyphosphoryl)oxy)phenyl)acrylate 

Relevant academic research and scientific papers

Evaluation of phosphoramidon and three synthetic phosphonates for inhibition of botulinum neurotoxin B catalytic activity

Three putative metalloprotease inhibitors were synthesized and tested for their ability to inhibit the catalytic activity of botulinum neurotoxin B light chain (BoNT/B LC). The compounds were designed to emulate the naturally occurring metalloprotease inhibitor phosphoramidon, which has been reported to be a weak antagonist of BoNT/B action. All three analogs contained the dipeptide Phe-Glu in place of Leu-Trp of phosphoramidon and possessed a phenyl, ethyl or methyl group in place of the rhamnose sugar of the parent compound. The inhibitors were evaluated in a cell-free assay based on the detection of a fluorescent product following cleavage of a 50-mer synaptobrevin peptide ([Pya88] S 39-88) by BoNT/B LC. This peptide corresponds to the hydrophilic core of synaptobrevin-2 and contains a fluorescent analog L-pyrenylalanine (Pya) in place of Tyr88. Cleavage of [Pya88] S 39-88 by BoNT/B LC gives rise to fragments of 38 and 12 amino acid residues. Quantification of BoNT/B-mediated substrate cleavage was achieved by separating the 12-mer fragment (FETSAAKLKRK-Pya) that contains the C-terminal fluorophore and measuring fluorescence at 377 nm. The results indicate that the phenyl-substituted synthetic compound ICD 2821 was slightly more active than phosphoramidon, but analogs with methyl or ethyl substitutions were relatively inactive. These findings suggest that phosphonate monoesters may be useful for providing insights into the structural requirement of BoNT/B protease inhibitors.

Aryloxy Pivaloyloxymethyl Prodrugs as Nucleoside Monophosphate Prodrugs

Intracellular phosphorylation of therapeutic nucleoside analogues into their active triphosphate metabolites is a prerequisite for their pharmacological activity. However, the initial phosphorylation of these unnatural nucleosides into their monophosphate derivatives can be a rate-limiting step in their activation. To address this, we herein report the development of the aryloxy pivaloyloxymethyl prodrugs (POMtides) as a novel and effective nucleoside monophosphate prodrug technology and its successful application to the anticancer nucleoside analogue 5-fluoro-2′-deoxyuridine (FdUR).

Palladium-catalyzed ortho-alkenylation of aryl hydrogen phosphates using a new mono-phosphoric acid directing group

A highly efficient Pd-catalyzed ortho-alkenylation is reported using a mono-phosphoric acid-directing group for the first time. This phosphoric acid-directing group is successfully utilized for the synthesis of various alkenylated products and offers a new approach to transition-metal-catalyzed C-H activation. The Royal Society of Chemistry 2013.

Pd(II)-catalyzed ortho-arylation of aryl phosphates and aryl hydrogen phosphates with diaryliodonium triflates

Functionalized biaryl compounds were successfully synthesized using phosphates as the ortho-directing group in the Pd(II)/Pd(IV) catalytic cycle.