7331-13-7Relevant articles and documents
Effect of phosphate activating group on oligonucleotide formation on montmorillonite: The regioselective formation of 3′,5′-linked oligoadenylates
Prabahar, K. Joseph,Cole, Timothy D.,Ferris, James P.
, p. 10914 - 10920 (1994)
The effects of amine structure on the montmorillonite-catalyzed oligomerization of the 5′-phosphoramidates of adenosine are investigated. 4-Aminopyridine derivatives yielded oligoadenylates as long as dodecamers with a regioselectivity for 3′,5′-phosphodiester bond formation averaging 88%. Linear and cyclic oligomers are obtained and no A5′ppA-containing products are detected. Oligomers as long as the hexanucleotide are obtained using 2-aminobenzimidazole as the activating group. A predominance of pA2′pA is detected in the dimer fraction along with cyclic 3′,5′-trimer; no A5′ppA-containing oligomers were detected. Little or no oligomer formation was observed when morpholine, piperidine, pyrazole, 1,2,4-triazole, and 2-pyridone are used as phosphate-activating groups. The effects of the structure of the phosphate activating group on the oligomer structure and chain lengths are discussed.
5′-β,γ-CHF-ATP Diastereomers: Synthesis and Fluorine-Mediated Selective Binding by c-Src Protein Kinase
Hwang, Candy S.,Kung, Alvin,Kashemirov, Boris A.,Zhang, Chao,McKenna, Charles E.
supporting information, p. 1624 - 1627 (2015/04/14)
The first preparation of the individual β,γ-CHF-ATP stereoisomers 12a and 12b is reported. Configurationally differing solely by the orientation of the C-F fluorine, 12a and 12b have discrete 31P (202 MHz, pH 10.9, ΔδPα 6 Hz, ΔδPβ 4 Hz) and 19F NMR (470 MHz, pH 9.8, ΔδF 25 Hz) spectral signatures and exhibit a 6-fold difference in IC50 values for c-Src kinase, attributed to a unique interaction of the (S)-fluorine of bound 12b with R388 in the active site.
Rapid synthesis of Abelson tyrosine kinase inhibitors using click chemistry
Kalesh, Karunakaran A.,Liu, Kai,Yao, Shao Q.
experimental part, p. 5129 - 5136 (2010/04/04)
Protein kinases catalyze the phosphorylation of serine, threonine, tyrosine and histidine residues in proteins. Aberrant regulation of kinase activity has been implicated in many diseases including cancer. Thus development of new strategies for kinase inhibitor design remains an active area of research with direct relevance to drug development. Abelson (Abl) tyrosine kinase is one of the Src-family of tyrosine kinases and is directly implicated in Chronic Myelogenous Leukemia (CML). In this article, we have, for the first time, developed an efficient method for the construction of small molecule-based bisubstrate inhibitors of Abl kinase using click chemistry. Subsequent biochemical screenings revealed a set of moderately potent inhibitors, a few of which have comparable potency to Imatinib (an FDA-approved drug for treatment of chronic myeloid leukemia) against Abl.