siRNA potency enhancement via chemical modifications of nucleotide bases at the 5'-end of the siRNA guide strand

RNA. 2021 Feb;27(2):163-173. doi: 10.1261/rna.073783.119. Epub 2020 Nov 11.

Abstract

Small interfering RNAs (siRNAs) can be utilized not only as functional biological research tools but also as therapeutic agents. For the clinical use of siRNA as drugs, various chemical modifications have been used to improve the activity of siRNA drugs, and further chemical modifications are expected to improve the utility of siRNA therapeutics. As the 5' nucleobase of the guide strand affects the interaction between an siRNA and AGO2 and target cleavage activity, structural optimization of this specific position may be a useful strategy for improving siRNA activity. Here, using the in silico model of the complex between human AGO2 MID domain and nucleoside monophosphates, we screened and synthesized an original adenine-derived analog, 6-(3-(2-carboxyethyl)phenyl)purine (6-mCEPh-purine), that fits better than the natural nucleotide bases into the MID domain of AGO2. Introduction of the 6-mCEPh-purine analog at the 5'-end of the siRNA guide strand significantly enhanced target knockdown activity in both cultured cell lines and in vivo animal models. Our findings can help expand strategies for rationally optimizing siRNA activity via chemical modifications of nucleotide bases.

Keywords: Argonaute; RISC; RNA silencing; chemical modification; drug delivery; siRNA.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenine / analogs & derivatives
  • Adenine / chemical synthesis
  • Adenine / pharmacology*
  • Adenosine Monophosphate / chemistry
  • Adenosine Monophosphate / metabolism
  • Animals
  • Apolipoprotein B-100 / antagonists & inhibitors
  • Apolipoprotein B-100 / blood
  • Apolipoprotein B-100 / chemistry
  • Apolipoprotein B-100 / genetics
  • Argonaute Proteins / genetics*
  • Argonaute Proteins / metabolism
  • Base Pairing
  • Base Sequence
  • Binding Sites
  • Cholesterol / blood
  • HeLa Cells
  • Humans
  • Hydrogen Bonding
  • Hydrophobic and Hydrophilic Interactions
  • Male
  • Methylation
  • Mice
  • Mice, Knockout
  • Models, Molecular
  • Protein Binding
  • RNA Interference / drug effects*
  • RNA, Double-Stranded / genetics*
  • RNA, Double-Stranded / metabolism
  • RNA, Small Interfering / agonists*
  • RNA, Small Interfering / genetics
  • RNA, Small Interfering / metabolism
  • RNA-Induced Silencing Complex / agonists*
  • RNA-Induced Silencing Complex / genetics
  • RNA-Induced Silencing Complex / metabolism
  • Uridine Monophosphate / chemistry
  • Uridine Monophosphate / metabolism

Substances

  • AGO2 protein, human
  • Apob protein, mouse
  • Apolipoprotein B-100
  • Argonaute Proteins
  • RNA, Double-Stranded
  • RNA, Small Interfering
  • RNA-Induced Silencing Complex
  • Adenosine Monophosphate
  • Cholesterol
  • Uridine Monophosphate
  • Adenine