DNTP MODIFIED AT TRIPHOSPHATE RESIDUES - SUBSTRATE PROPERTIES TOWARDSDNA-POLYMERASES AND STABILITY IN HUMAN SERUM

Substrate and terminating substrate properties of dNTP with phosphate groups replaced by phosphonates at alpha-, gamma-, beta,gamma-, and al pha,beta,gamma-positions towards different human DNA polymerases and r etroviral reverse transcriptases are reviewed. Substitution of the pho sphate group by the phosphonate at any of the three phosphate position s of dNTP increased their stability towards dephosphorylating enzymes of human blood. In some cases hydrophobicity of these compounds was ma rkedly enhanced.