Abstract
NF-κB transcription factors include a group of five mammalian proteins that form hetero- or homodimers and regulate hundreds of target genes involved in acute inflammation, HIV-1 transcription activation, and resistance to cancer therapy. We previously used in vitro selection to develop a small RNA aptamer (anti-p50) that binds the DNA-binding domain of NF-κB p50 2 with low nanomolar affinity but does not bind NF-κB p65 2. Here, we report the in vitro selection of anti-NF-κB p65 RNA aptamers using parallel in vitro selections with either a fully randomized RNA library or a degenerate RNA library based on the primary sequence of the 31-nucleotide anti-p50 RNA aptamer. We report the characterization of these aptamers with respect to NF-κB target specificity, affinity, minimal sequence requirements, secondary structure, and competition with DNA κB sites. These results expand opportunities for artificial inhibition of NF-κB transcription factor dimers containing p65 subunits. Published by Cold Spring Harbor Laboratory Press.
Original language | English (US) |
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Pages (from-to) | 1037-1047 |
Number of pages | 11 |
Journal | RNA |
Volume | 14 |
Issue number | 6 |
DOIs | |
State | Published - Jun 2008 |
Keywords
- Aptamer
- In vitro selection
- NF-κB
- p65
ASJC Scopus subject areas
- Molecular Biology