Cyclic Amide-Linked Oxazolidinone Triazoles as Inhibitors of the T-Box Riboswitch
Antimicrobial resistance remains a critical global health challenge, and was intensified by the COVID-19 pandemic. To address this growing threat, novel antibacterial agents targeting unconventional mechanisms are urgently needed. One promising strategy involves inhibiting bacterial riboswitches-RNA elements that regulate gene expression. Unlike most riboswitches that respond to small-molecule metabolites, the T-box riboswitch uniquely binds non-aminoacylated tRNA and is predominantly found in Gram-positive bacteria, making it an attractive target due to its conserved sequences and regulatory role over essential genes. This study explored oxazolidinone- and triazole-based compounds as potential inhibitors of the T-box riboswitch. Prior investigations into tricyclic oxazolidinones revealed an allosteric modulator that effectively inhibited T-box riboswitch transcriptional readthrough in vitro, though it showed limited disruption of the isolated tRNA-antiterminator complex. To enhance RNA-binding affinity and stereoselectivity, a macrocyclic oxazolidinone scaffold was designed, incorporating a strategic substituent to expand the interaction footprint. A synthetically viable candidate was identified, and computational docking studies suggested that one of the designed compounds may interfere with tRNA-induced transcription by forming π-π stacking interactions with G5 in the antiterminator region. These findings support the potential of targeting the T-box riboswitch with structurally optimized small molecules as a novel antibacterial strategy.
Authors
- Jessica M. Roberts (ORCID: https://orcid.org/0000-0003-3164-7256)
- Ali H. Aldhumani (ORCID: https://orcid.org/0000-0002-1898-8147)
- Emily A. Fairchild (ORCID: https://orcid.org/0000-0002-0226-6801)
- Jennifer V. Hines (ORCID: https://orcid.org/0000-0001-9812-3137)
- Stephen C Bergmeier
- Eric Parsons
- Oluwaseun B. Adegbite
Institutions
- Ohio University (US)
Publication Details
- Journal
- Molecules
- Published
- 2025-12-22
- DOI
- https://doi.org/10.3390/molecules31010029
- Primary Topic
- RNA and protein synthesis mechanisms
- Type
- article
- Field-Weighted Citation Impact
- 0.00