dNTP Modified at Triphosphate Residues: Substrate Properties Towards DNA Polymerases and Stability in Human Serum

Abstract

Substrate and terminating substrate properties of dNTP with phosphate groups replaced by phosphonates at α-, γ-, β,γ-, and α,β,γ-positions towards different human DNA polymerases and retroviral reverse transcriptases are reviewed. Substitution of the phosphate group by the phosphonate at any of the three phosphate positions of dNTP increased their stability towards dephosphorylating enzymes of human blood. In some cases hydrophobicity of these compounds was markedly enhanced.