Promising Target in Fight Against Bacteria
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A research group at Tohoku University has made a significant discovery with positive implications for the development of bacteria-fighting drugs. The aminoacyl-tRNA site (A-site) of the 16S RNA decoding region in the bacterial ribosome looks promising for a new era of antibiotic drug development.
Traditional aminoglycoside antibiotics are problematic given their high toxicity and the potential for resistance development. The research at Tohoku University focused on bacterial A-site binding small ligands whose structures are distinct from the aminoglycoside family, which offer potential for the development of novel drugs that treat bacterial infections with a reduction in the problems associated with traditional antibiotics.
The research group led by Dr. Seiichi Nishizawa and Dr. Yusuke Sato (Department of Chemistry, Graduate School of Science) has reported a novel small ligand, ATMND-C2-NH2 that has the tightest binding affinity for the bacterial A-site among the non-aminoglycoside ligands.
ATMND-C2-NH2 shows a significant fluorescent quenching response upon selective binding to the internal loop of the bacterial (Escherichia coli) A-site-containing model RNA.
ATMND-C2-NH2 has also proven useful as an indicator for assessing ligand/A-site interactions.
The results obtained by the research group offer a rational basis for the generation of novel A-site binding ligands with a view toward novel antibiotics with less toxicity and minimum resistance development.
This article has been republished from materials provided by Tohoku University. Note: material may have been edited for length and content. For further information, please contact the cited source.
Reference
Fluorescent Trimethylated Naphthyridine Derivative with an Aminoalkyl Side Chain as the Tightest Non‐aminoglycoside Ligand for the Bacterial A‐site RNA. Yusuke Sato, Masafumi Rokugawa, Sho Ito, Sayaka Yajima, Hiroki Sugawara, Norio Teramae, Seiichi Nishizawa. Volume 24, Issue 52, September 18, 2018, Pages 13862-13870, https://doi.org/10.1002/chem.201802320.
