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The proliferation of germs that are resistant to antibiotics poses a significant risk to public health. The majority of antibiotics used now only affect a small number of metabolic pathways, which promotes antibiotic resistance. As a direct result of this, innovative regulatory inhibitory methods are required. Riboswitches are an interesting potential target for the development of antibacterial medicines. Purine riboswitches are an intriguing topic to discuss due to the crucial functions that they play in the genetic regulation of metabolic processes in bacteria. Class I (2′-dG-I) and class II (2′-dG-II) riboswitches are examples of the several types of 2′- deoxyguanosine (2′-dG) riboswitches that are involved in the regulation of deoxyguanosine metabolism. On the other hand, a high affinity for nucleosides requires either local or distal changes around the ligand-binding pocket, and this varies from class to class. Therefore, it is absolutely necessary to get an understanding of the recognition mechanisms utilized by these riboswitches while acting as antibiotic targets. In this study, we investigated the structure, dynamics, and energy landscape of both classes of 2′-dG that were attached to the nucleoside ligands, 2′-deoxyguanosine and riboguanosine, using a variety of computational biophysics techniques. According to the findings of this study, a higher nucleoside ligand affinity is associated with enhanced stability as well as an increase in the number of contacts that take place in the three-way junction where 2′-dG riboswitches are located. Additionally, alterations in the structure of the 2′-dG-II aptamers make it possible for improved intramolecular communication. In general, the fact that the 2′-dG-II riboswitch is able to identify cognate as well as noncognate ligands makes it a potentially useful target for the design of drugs.

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1	Deborah Santos(deborah.antuness@gmail.com)
2	Lucianna Santos(luciannahss@gmail.com)
3	Ernesto Caffarena(ernesto.caffarena@fiocruz.br)
4	Ana Carolina Guimarães(acarol.guimaraes@gmail.com)

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