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 |
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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
Cite this
Screening helix-threading peptides for RNA binding using a thiazole orange displacement assay. / Krishnamurthy, Malathy; Schirle, Nicole T.; Beal, Peter A.
In: Bioorganic and Medicinal Chemistry, Vol. 16, No. 19, 01.10.2008, p. 8914-8921.Research output: Contribution to journal › Article
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TY - JOUR
T1 - Screening helix-threading peptides for RNA binding using a thiazole orange displacement assay
AU - Krishnamurthy, Malathy
AU - Schirle, Nicole T.
AU - Beal, Peter A.
PY - 2008/10/1
Y1 - 2008/10/1
N2 - 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.
AB - 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.
KW - Cyclic peptides
KW - High-throughput screening
KW - RNA recognition
KW - Threading intercalation
UR - http://www.scopus.com/inward/record.url?scp=52949100972&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=52949100972&partnerID=8YFLogxK
U2 - 10.1016/j.bmc.2008.08.066
DO - 10.1016/j.bmc.2008.08.066
M3 - Article
C2 - 18789700
AN - SCOPUS:52949100972
VL - 16
SP - 8914
EP - 8921
JO - Bioorganic and Medicinal Chemistry
JF - Bioorganic and Medicinal Chemistry
SN - 0968-0896
IS - 19
ER -