Chemical modification of hammerhead ribozymes. Catalytic activity and nuclease resistance

J Biol Chem. 1995 Oct 27;270(43):25702-8. doi: 10.1074/jbc.270.43.25702.

Abstract

A systematic study of selectively modified, 36-mer hammerhead ribozymes has resulted in the identification of a generic, catalytically active and nuclease stable ribozyme motif containing 5 ribose residues, 29-30 2'-O-Me nucleotides, 1-2 other 2'-modified nucleotides at positions U4 and U7, and a 3'-3'-linked nucleotide "cap." Eight 2'-modified uridine residues were introduced at positions U4 and U7. From the resulting set of ribozymes, several have almost wild-type catalytic activity and significantly improved stability. Specifically, ribozymes containing 2'-NH2 substitutions at U4 and U7, or 2'-C-allyl substitutions at U4, retain most of their catalytic activity when compared to the all-RNA parent. Their serum half-lives were 5-8 h in a variety of biological fluids, including human serum, while the all-RNA parent ribozyme exhibits a stability half-life of only approximately 0.1 min. The addition of a 3'-3'-linked nucleotide "cap" (inverted T) did not affect catalysis but increased the serum half-lives of these two ribozymes to > 260 h at nanomolar concentrations. This represents an overall increase in stability/activity of 53,000-80,000-fold compared to the all-RNA parent ribozyme.

Publication types

  • Comparative Study

MeSH terms

  • Animals
  • Base Sequence
  • Blood / metabolism
  • Catalysis
  • Cattle
  • Half-Life
  • Humans
  • Molecular Sequence Data
  • Nucleosides / chemistry
  • RNA, Catalytic / chemistry*
  • RNA, Catalytic / metabolism*
  • RNA, Catalytic / pharmacokinetics
  • Ribonucleases / metabolism
  • Structure-Activity Relationship

Substances

  • Nucleosides
  • RNA, Catalytic
  • Ribonucleases