1608113-92-3

Upstream product

• 50-89-5 thymidine 
• 108549-23-1 Dibenzyl N,N-diisopropylphosphoramidite 
• 40733-27-5 3'-O-(t-butyldimethylsilyl)thymidine 
• 40733-26-4 3',5'-O-di(tert-butyldimethylsilyl)thymidine 

Downstream Products

• 1608113-31-0 C₄₄H₅₃N₆O₁₄P 
• 5115-07-1 O,O-dibenzyl O-(5'-deoxythymidine-5'-yl)phosphate 
• 1608113-35-4 C₃₁H₃₀N₃O₁₂P 
• 1608113-36-5 C₄₁H₄₇N₆O₁₄P 
• 1608113-37-6 C₄₇H₅₉N₆O₁₄PS 
• 1608113-38-7 C₄₁H₅₅N₆O₁₄PS 
• 1608113-39-8 C₅₂H₆₈N₇O₁₆PS 
• 1608113-40-1 C₄₃H₅₉N₆O₁₅P 
• 1608113-41-2 C₃₈H₅₀N₅O₁₃PS 
• 1608113-42-3 C₅₀H₆₄N₇O₁₅PS 
• 1608113-44-5 C₅₃H₆₉N₈O₁₆PS 
• 1608113-86-5 C₅₂H₇₆N₇O₁₆PS 
• 33430-62-5 thymidine 5'-phosphate sodium salt 

Relevant academic research and scientific papers

5’-Phosphorylation Increases the Efficacy of Nucleoside Inhibitors of the DNA Repair Enzyme SNM1A

Certain cancers exhibit upregulation of DNA interstrand crosslink repair pathways, which contributes to resistance to crosslinking chemotherapy drugs and poor prognoses. Inhibition of enzymes implicated in interstrand crosslink repair is therefore a promising strategy for improving the efficacy of cancer treatment. One such target enzyme is SNM1A, a zinc co-ordinating 5’–3’ exonuclease. Previous studies have demonstrated the feasibility of inhibiting SNM1A using modified nucleosides appended with zinc-binding groups. In this work, we sought to develop more effective SNM1A inhibitors by exploiting interactions with the phosphate-binding pocket adjacent to the enzyme's active site, in addition to the catalytic zinc ions. A series of nucleoside derivatives bearing phosphate moieties at the 5’-position, as well as zinc-binding groups at the 3’-position, were prepared and tested in gel-electrophoresis and real-time fluorescence assays. As well as investigating novel zinc-binding groups, we found that incorporation of a 5’-phosphate dramatically increased the potency of the inhibitors.

Tailoring peptide-nucleotide conjugates (PNCs) for nucleotide delivery in bacterial cells

The design and synthesis of peptide-2′-deoxythymidine-5′-O- monophosphate conjugates as potential active delivery systems for nucleotides into auxotrophic E. coli strains is presented. A series of oligopeptides were allowed to react with 5′-O-(dibenzylphosphate)-2′-deoxythymidine or its suitably 3′-derivatized analogues to give the relevant peptide-nucleotide adducts, by the formation of a biolabile chemical connection. Using strategies based on the principles of orthogonal protection and activation, rational variations were made to the linker and the peptide moiety in order to tune the metabolic stability of the conjugates.