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• W2161536758 abstract "The kinetics of the complementary 15mer RNA (3) cleavage by RNase H in the conformationally-constrained [North-East type sugar constraint] triple oxetane modified antisense oligonucleotide AON (2)–RNA (3) hybrid duplexes (P. I. Pradeepkumar and J. Chattopadhyaya, J. Chem. Soc., Perkin Trans. 2, 2001, 2074) have been investigated, in comparison with the native 15mer counterpart AON (1)–RNA (3), by changing both AON and RNA concentrations, while keeping the enzyme and buffer concentrations constant. The RNA concentration-dependent kinetics of the RNase H promoted cleavage reaction gave values for Km and Vmax for both substrates: AON (1)–RNA (3) and AON (2)–RNA (3) heteroduplexes. The Vmax and the Km values were respectively ∼2 and ∼10 times greater for the AON (2)–RNA (3) duplex than those for the native counterpart, which means that the incorporation of the North-East type sugar constrained triple oxetane modifications in the AON increases the catalytic activity of RNase H by almost ca. 2-fold owing to the decreased affinity of the substrate toward the enzyme. The Tm for the AON (2)–RNA (3) hybrid duplex was 18 °C less than that of the native. Thus, an inverse correlation between AON–RNA hybrid duplex thermostability and RNase H activity has been found under the high substrate concentration conditions. Under high substrate concentration conditions, the RNase H activity of the AON (2)–RNA (3) hybrid duplex is however higher than the native because of a more rapid turn over (Nmax) of RNase H. Conversely, under low substrate concentration conditions, the RNase H activity of AON (2)–RNA (3) hybrid duplex dramatically drops compared to the native because of the less effective turn over (Neff) of enzyme. This is because the Neff, under low substrate concentration conditions, depends on maximal turn over, Nmax, as well as on the extent of saturation of enzyme by substrate, which in turn depends upon the value of the Vmax/Km ratio, which for the AON (2)–RNA (3) hybrid duplex has been found to be ∼4-fold less than the native." @default.
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• W2161536758 date "2002-03-20" @default.
• W2161536758 modified "2023-09-27" @default.
• W2161536758 title "Kinetic analysis of the RNA cleavage of the conformationally-constrained oxetane-modified antisense-RNA hybrid duplex by RNase HElectronic supplementary information (ESI) available: autoradiograms of denaturing PAGE gels. See http://www.rsc.org/suppdata/p2/b1/b111438g/" @default.
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• W2161536758 doi "https://doi.org/10.1039/b111438g" @default.
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