1609462-52-3

Upstream product

• 1609462-44-3 (S)-allyl 2-{(tert-butoxycarbonyl)amino}-3-[4-{(diethoxyphosphoryl)difluoromethyl}phenyl]propanoate 
• 1609462-46-5 (S)-allyl 2-([{(9H-fluoren-9-yl)methoxy}carbonyl]amino)-3-[4-{(diethoxyphosphoryl)difluoromethyl}phenyl]propanoate 
• 612-25-9 2-Nitrobenzyl alcohol 
• 1609462-49-8 (S)-([4-{2-([{(9H-fluoren-9-yl)methoxy}carbonyl]amino)-3-(allyloxy)-3-oxopropyl}phenyl]difluoromethyl)phosphonic acid 
• 150618-05-6 (2S)-2-[(tert-butoxycarbonyl)amino]-3-{4-[(diethoxyphosphoryl)(difluoro)methyl]phenyl}propanoic acid 

Downstream Products

• 1609462-55-6 (2S)-2-([{(9H-fluoren-9-yl) methoxy}carbonyl]amino)3-{4-(difluoro[hydroxy{(2-nitro-benzyl)oxy}phosphoryl] methyl)-phenyl}propanoic acid 

Relevant academic research and scientific papers

Development of caged non-hydrolyzable phosphoamino acids and application to photo-control of binding affinity of phosphopeptide mimetic to phosphopeptide-recognizing protein

The design and synthesis of caged non-hydrolyzable phospho-serine, -threonine, and -tyrosine derivatives that generate parent non-hydrolyzable phosphoamino acids, containing a difluoromethylene unit instead of the oxygen of a phosphoester, after UV-irradiation are described. The caged non-hydrolyzable amino acids were incorporated into peptides by standard Fmoc solid-phase peptide synthesis, and the obtained peptides were successfully converted to the parent non-hydrolyzable phosphopeptides by UV-irradiation. Application of the caged non-hydrolyzable phosphoserine-containing peptide to photo-control the binding affinity of the peptide to 14-3-3β protein is also reported.