Screening helix-threading peptides for RNA binding using a thiazole orange displacement assay.

Screening helix-threading peptides for RNA binding using a thiazole orange displacement assay.
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DOI:
10.1016/j.bmc.2008.08.066
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发表时间:
2008-10-01
影响因子:
3.5
通讯作者:
Beal PA
Beal PA
中科院分区:
医学3区
文献类型:
--
作者:
Krishnamurthy M;Schirle NT;Beal PA

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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 (versus linear peptides), but independent of macrocyclic ring size for the penta-, tetra- and tri peptides analyzed.
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