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. 2010 Oct 4;49(41):7481-5.
doi: 10.1002/anie.201003168.

Selective modulation of DNA polymerase activity by fixed-conformation nucleoside analogues

Robert L Eoff  1 , Colleen E McGrath, Leena Maddukuri, S Giovanna Salamanca-Pinzón, Victor E Marquez, Lawrence J Marnett, F Peter Guengerich, Martin Egli
Affiliations

Selective modulation of DNA polymerase activity by fixed-conformation nucleoside analogues

Robert L Eoff et al. Angew Chem Int Ed Engl. .
No abstract available

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Figures

Figure 1
Figure 1
Chemical structure of N-MC-dATP 1 and S-MC-dATP 2, which mimic the sugar pucker observed in A- and B-form double-stranded nucleic acid helices, respectively.
Figure 2
Figure 2
DNA polymerase-catalyzed insertion and extension from fixed conformation nucleoside analogues. a) The primer-template DNA sequence is shown in schematic form. b) Full-length extension products for three human Y-family DNA polymerases. Catalysis was performed in the presence of dATP, N-MC-dATP, or S-MC-dATP and the other three dNTPs and the products were analyzed by PAGE.
Figure 3
Figure 3
Selective growth inhibition of cells over-expressing human DNA polymerase ι using fixed conformation nucleosides. a) Hs578T cells were exposed to varying concentrations of N-MC-dATP and then plated at a density of (□) 25,000, (○) 10,000, (■) 1,000, and (●) 500 cells/well. Hs578Bst (blue) and Hs578T (red) were exposed to varying concentrations of N-MC-dATP (b) or (c) HNE in order to measure the IC50 value.
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