Combinatorial selection and delivery of thioaptamers

Biochem Soc Trans. 2007 Feb;35(Pt 1):50-2. doi: 10.1042/BST0350050.

Abstract

Oligonucleotide-based agents are emerging as potential therapeutic agents that can be attractive alternatives for the small-molecule chemical drugs. Monothiophosphate-backbone-modified DNA aptamers (thioaptamers) that specifically and tightly bind to the RNase H domain of the HIV RT (reverse transcriptase) have been isolated from nucleic acid libraries using combinatorial selection methods. The selected thioaptamer inhibited RNase H activity of the HIV RT in in vitro studies. In cell cultures, the transfected thioaptamer markedly reduced HIV production in a dose-dependent manner. Gel electrophoretic mobility-shift assays and NMR spectroscopy showed that the selected thioaptamer binds to the isolated RNase H domain, but did not bind to a structurally similar RNase H from Escherichia coli. In cell cultures, the transfected thioaptamer showed a dose-dependent inhibition of HIV replication, with a maximal inhibition of 83%. Using various liposome-delivery agents, the DNA thioaptamer was transfected into HIV-infected astrocytoma adherent cells with greater than 70% efficiency.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Aptamers, Nucleotide / administration & dosage*
  • Aptamers, Nucleotide / chemistry*
  • Combinatorial Chemistry Techniques*
  • Escherichia coli / enzymology
  • Gene Transfer Techniques*
  • Genetic Techniques
  • HIV / metabolism
  • Humans
  • Liposomes / chemistry
  • Magnetic Resonance Spectroscopy
  • Models, Biological
  • Protein Binding
  • Protein Folding
  • Protein Structure, Tertiary
  • Ribonuclease H / chemistry
  • Ribonuclease H / metabolism
  • Transfection

Substances

  • Aptamers, Nucleotide
  • Liposomes
  • Ribonuclease H