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Updated: Apr 21, 2026

Optical Tweezers to Study RNA-Protein Interactions in Translation Regulation
Published on: February 12, 2022
Surface plasmon resonance--more than a screening technology: insights in the binding mode of σ70:core RNAP inhibitors
Kristina Hüsecken1, Stefan Hinsberger, Walid A M Elgaher
1Department of Drug Design & Optimization, Helmholtz Institute for Pharmaceutical Research Saarland (HIPS), Campus C2.3, D-66123 Saarbrücken, Germany.
Aim:
Antibiotic resistance has become a major health problem. The σ(70):core interface of bacterial RNA polymerase is a promising drug target. Recently, the coiled-coil and lid-rudder-system of the β' subunit has been identified as an inhibition hot spot. Materials & methods & Results: By using surface plasmon resonance-based assays, inhibitors of the protein-protein interaction were identified and competition with σ(70) was shown. Effective inhibition was verified in an in vitro transcription and a σ(70):core assembly assay. For one hit series, we found a correlation between activity and affinity. Mutant interaction studies suggest the inhibitors' binding site.
Conclusion:
Surface plasmon resonance is a valuable technology in drug design, that has been used in this study to identify and evaluate σ(70):core RNA polymerase inhibitors.
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