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An optimized synthetic route to 7-deaza-8-bromo-cyclic adenosine 5'-diphosphate ribose (7-deaza-8-bromo-cADPR 3), an established cell-permeant, hydrolysis-resistant cyclic adenosine 5'-diphosphate ribose (cADPR) antagonist, is presented. Using NMR analysis, we found that 3 adopted a C-2' endo conformation in the N9-linked ribose and a syn conformation about the N9-glycosyl linkage, which are similar to that of cADPR. The synthetic route was also employed to produce 7-deaza-2'-deoxy-cADPR 4, a potential cell-permeant cADPR analogue. 3 and 4 were more stable to chemical hydrolysis, consistent with the observation that 7-deaza-cADPR analogues are more stable than their parent adenosine derivatives. 3 was also found to be stable to enzyme-mediated hydrolysis using CD38 ectoenzyme.

Original publication

DOI

10.1021/jo071236p

Type

Journal article

Journal

J Org Chem

Publication Date

07/03/2008

Volume

73

Pages

1693 - 1703

Keywords

Calcium, Cell Membrane Permeability, Chromatography, High Pressure Liquid, Cyclic ADP-Ribose, Hydrolysis, Magnetic Resonance Spectroscopy, Mass Spectrometry, Molecular Conformation