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• W1979807584 abstract "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." @default.
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• W1979807584 date "2014-09-01" @default.
• W1979807584 modified "2023-09-27" @default.
• W1979807584 title "Surface plasmon resonance – more than a screening technology: insights in the binding mode of σ⁷⁰:core RNAP inhibitors" @default.
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• W1979807584 doi "https://doi.org/10.4155/fmc.14.105" @default.
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