Search

This article discusses the usage of modified methyl phosphonate oligonucleotides as antisense and antigene agents. Results show that the R(sub)p and S(sub)p diastereomers exhibit different hybridization capabilities of the methylphosphonate strand.

Structural similarities of MutT and the C-terminal domain of MutY of Escherichia coli are discussed based on NMR study which found striking similarity in the domain vs the reported solution structure of MutT. They have similar topology, and secondary structure elements are arranged in like ways in the two proteins.

The study employs a two-step process, which helps in the identification of special monothiophosphate-modified aptamers (thioaptamers) that can bind to the hyaluronic acid binding domain (HBAD). These thioaptamers are shown to be extremely beneficial and can be used as a targeting agent during the delivery of therapeutic payloads.

A few inhibitors of RNase H are reported, despite the key role played by the RNase H of human immunodeficiency virus-1 reverse transcriptase (HIV-1 RT) in viral proliferation. Double-stranded DNA thioaptamers that inhibit RNase H activity and viral replication are selected using in vitro combinational selection methods and the RNase H domain of the HIV RT.

Results reveal that both cis- and trans-opened (10R)-dA adducts in duplex oligonucleotides, from benzo[a]pyrene and benzo-ring 7,8-diol 9.10-epoxides (DE), exhibit aromatic hydrocarbon intercalated into the DNA on the 5'-side of the modified adenine. The solution structure and conformation of an 11-meroligonucleotide duplex containing the DE adduct are presented.