ORGN 389 |
| Ever increasing evidence indicates that RNA performs a wide range of cellular functions independent of its role as a carrier for genetic information. Small molecules that can specifically target RNA have the potential to regulate RNA-mediated functions and provide new avenues for therapeutic treatments. The increased specificity, stability, and bioavailability of cyclic peptides offer a unique solution to the design of RNA-binding small molecules. To identify novel cyclic peptide scaffolds, a cysteine constrained heptapeptide phage display library was panned against BIV-TAR. After multiple rounds of positive and negative selection, a pool of sequence specific binders were identified. Competitive gel shift analysis that measured the ability of the isolated cyclic peptides to disrupt the Tat-TAR interaction was then employed to confirm biological activity. This methodology enables the rapid identification of novel cyclic peptide scaffolds as potential ligands to explore small molecule control of RNA-mediated cellular functions. |
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New Reactions and Methodology, Bioorganic Chemistry, Molecular Recognition and Self Assembly
8:00 PM-10:00 PM, Tuesday, 28 March 2006 Georgia World Congress Center -- Ex. Hall B4, Poster
Sci-Mix
Division of Organic Chemistry |