ArticleBioorganic & medicinal chemistry2013
Selection of heptapeptides that bind helix 69 of bacterial 23S ribosomal RNA.
Article in Bioorganic & medicinal chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
4 citing papers in PubMed.
- Peptides Targeting RNA mChemMedChem · 2023Article
- Discovery of a novel small molecular peptide that disrupts helix 34 of bacterial ribosomal RNA.RSC advances · 2019Article
- The development of peptide ligands that target helix 69 rRNA of bacterial ribosomes.Bioorganic & medicinal chemistry · 2016Article
- Synthetic RNA recognition motifs that selectively recognize HIV-1 trans-activation response element hairpin RNA.ACS chemical biology · 2014Article
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
Helix 69 of Escherichia coli 23S rRNA has important roles in specific steps of translation, such as subunit association, translocation, and ribosome recycling. An M13 phage library was used to identify peptide ligands with affinity for helix 69. One selected sequence, NQVANHQ, was shown through a bead assay to interact with helix 69. Electrospray ionization mass spectroscopy revealed an apparent dissociation constant for the amidated peptide and helix 69 in the low micromolar range. This value is comparable to that of aminoglycoside antibiotics binding to the A site of 16S rRNA or helix 69. Helix 69 variants (human) and unrelated RNAs (helix 31 or A site of 16S rRNA) showed two- to fourfold lower affinity for NQVANHQ-NH(2). These results suggest that the peptide has desirable features for development as a lead compound for novel antimicrobials.
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