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

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, alpha-amino acid stereochemistry, and cyclization (vs linear peptides), but independent of macrocyclic ring size for the penta-, tetra- and tri-peptides analyzed.

journal_name

Bioorg Med Chem

authors

Krishnamurthy M,Schirle NT,Beal PA

doi

10.1016/j.bmc.2008.08.066

subject

Has Abstract

pub_date

2008-10-01 00:00:00

pages

8914-21

issue

19

eissn

0968-0896

issn

1464-3391

pii

S0968-0896(08)00809-2

journal_volume

16

pub_type

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