151203-55-3

Upstream product

• 107-15-3 ethylenediamine 
• 129451-79-2 N-(9-{5-[bis(4-methoxyphenyl)phenylmethoxyphenyl]-4-hydroxytetrahydrofuran-2-yl}-8-bromo-9H-purin-6-yl)benzamide 
• 14985-44-5 8-bromo-2'-deoxyadenosine 
• 149540-21-6 5-(6-amino-8-bromo-9H-purin-9-yl)-2-((bis(4-methoxyphenyl)(phenyl)methoxy)methyl)tetrahydrofuran-3-ol 
• 129451-78-1 N-[8-Bromo-9-((2R,4S,5R)-4-hydroxy-5-hydroxymethyl-tetrahydro-furan-2-yl)-9H-purin-6-yl]-benzamide 
• 98-88-4 benzoyl chloride 
• 40615-36-9 4,4'-dimethoxytrityl chloride 

Downstream Products

• 151322-49-5 3'-O-acetyl-N⁶-benzoyl-8-amino(2-N-acetylaminoethyl)-2'-deoxyadenosine 
• 151322-50-8 C₆₀H₆₁ClN₉O₁₅P 

Relevant academic research and scientific papers

Influence of Linker Length on Ligase-Catalyzed Oligonucleotide Polymerization

Ligase-catalyzed oligonucleotide polymerization (LOOPER) that enables the sequence-defined generation of DNA with up to 16 different modifications has recently been developed. This approach was used to develop new classes of diversely modified DNA aptamer

Synthesis and conformational studies of d(TpA) and r(UpA) conjugated with histamine and ethylenediamine

Dinucleotides (Figure 1b-d) possessing histamino/ethylenediamino substituents at C8 of adenine have been synthesised for modelling the molecular interactions that occur at catalytic site of nucleases. These compounds have been designed for putative molecular recognition of internucleotide phosphate by a complementary group (imidazole/-NH2) in the pendant C-8 side chains. 1H NMR spectroscopic analysis of synthesised model compounds indicate that C-8 modification leads to increase in percentage of S conformation of modified sugar while still maintaining an anti glycosyl torsion as in unmodified analog d(TpA). The C-8 side chain functionality (histamine/ethylenediamine) is probably involved in intramolecular interaction (electrostatic/ hydrogen bond) with the phosphate and/or 2′OH in (14). Such predisposition of side chain catalytic groups is important in developing appropriate models for active site of nucleases.