Abstract
The fluorescent intercalator displacement assay using thiazole orange has been adapted to the study of RNA-binding helix-threading peptides (HTPs). This assay is highly sensitive with HTP-binding RNAs and provides binding affinity data in good agreement with quantitative ribonuclease footprinting without the need for radiolabeling or gel electrophoresis. The FID assay was used to define structure activity relationships for a small library of helix-threading peptides. Results of these studies indicate their RNA binding is dependent on peptide sequence, α-amino acid stereochemistry, and cyclization (vs linear peptides), but independent of macrocyclic ring size for the penta-, tetra- and tri-peptides analyzed.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 8914-8921 |
| Number of pages | 8 |
| Journal | Bioorganic and Medicinal Chemistry |
| Volume | 16 |
| Issue number | 19 |
| DOIs | |
| State | Published - Oct 1 2008 |
Keywords
- Cyclic peptides
- High-throughput screening
- RNA recognition
- Threading intercalation
ASJC Scopus subject areas
- Pharmaceutical Science
- Drug Discovery
- Organic Chemistry
- Molecular Medicine
- Molecular Biology
- Clinical Biochemistry
- Biochemistry
Fingerprint Dive into the research topics of 'Screening helix-threading peptides for RNA binding using a thiazole orange displacement assay'. Together they form a unique fingerprint.
Cite this
Krishnamurthy, M., Schirle, N. T., & Beal, P. A. (2008). Screening helix-threading peptides for RNA binding using a thiazole orange displacement assay. Bioorganic and Medicinal Chemistry, 16(19), 8914-8921. https://doi.org/10.1016/j.bmc.2008.08.066