Homodimerization is crucial for the regulation of numerous cellular processes. Enzymes often require dimerization for catalytic activity, thus fulfilling morphological functions is regulated by their oligomeric state. With the rise of antibiotic resistance and the emergence of new viruses, more research is focused on utilizing the dimerization surface as a potential target in drug development. Identifying novel dimerization inhibitors requires effective methods for screening libraries of small molecules, that allow the identification of the oligomeric state. With this thesis, we attempted to verify the potential of two systems for detecting homodimerization in Escherichia coli – namely LEXGFP and TOXGFP – as tolls for screening libraries of small molecule dimerization inhibitors in bacterial cells. We analysed the oligomeric state of four key bacterial or viral enzymes, for which dimerization inhibitors are known – Mpro protease from SARS-CoV-2, bacterial histidine kinase EnvZ from Escherichia coli, the cytomegalovirus protease, and the protease of the herpesvirus associated with Kaposi's sarcoma. We managed to confirm only the homodimerization of the first two. We then analysed their oligomeric state after the use of dimerization inhibitors. Statistically significant results were obtained only with the TOXGFP system, and further research is needed to confirm the usability of this system for screening libraries of dimerization inhibitors.
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