Synthesis, biophysical properties and biological activity of second generation antisense oligonucleotides containing chiral phosphorothioate linkages

Nucleic Acids Res. 2014 Dec 16;42(22):13456-68. doi: 10.1093/nar/gku1115. Epub 2014 Nov 14.

Abstract

Bicyclic oxazaphospholidine monomers were used to prepare a series of phosphorothioate (PS)-modified gapmer antisense oligonucleotides (ASOs) with control of the chirality of each of the PS linkages within the 10-base gap. The stereoselectivity was determined to be 98% for each coupling. The objective of this work was to study how PS chirality influences biophysical and biological properties of the ASO including binding affinity (Tm), nuclease stability, activity in vitro and in vivo, RNase H activation and cleavage patterns (both human and E. coli) in a gapmer context. Compounds that had nine or more Sp-linkages in the gap were found to be poorly active in vitro, while compounds with uniform Rp-gaps exhibited activity very similar to that of the stereo-random parent ASOs. Conversely, when tested in vivo, the full Rp-gap compound was found to be quickly metabolized resulting in low activity. A total of 31 ASOs were prepared with control of the PS chirally of each linkage within the gap in an attempt to identify favorable Rp/Sp positions. We conclude that a mix of Rp and Sp is required to achieve a balance between good activity and nuclease stability.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cells, Cultured
  • Fungal Proteins / metabolism
  • Mice
  • Oligonucleotides, Antisense / chemical synthesis
  • Oligonucleotides, Antisense / chemistry*
  • Oligonucleotides, Antisense / metabolism
  • Oligonucleotides, Antisense / pharmacology
  • Phosphorothioate Oligonucleotides / chemistry*
  • Ribonuclease H / metabolism
  • Single-Strand Specific DNA and RNA Endonucleases / metabolism
  • Stereoisomerism
  • Temperature

Substances

  • Fungal Proteins
  • Oligonucleotides, Antisense
  • Phosphorothioate Oligonucleotides
  • Ribonuclease H
  • Endonuclease S1, Aspergillus
  • Single-Strand Specific DNA and RNA Endonucleases