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Studies on the Conformational Features of Neomycin-B and its Molecular Recognition by RNA and Bacterial Defense Proteins

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Bioactive Conformation II

Part of the book series: Topics in Current Chemistry ((TOPCURRCHEM,volume 273))

Abstract

According to NMR and molecular dynamics simulations, the conformational behavior of natural aminoglycosidesis characterized by a remarkable flexibility, with different conformations, even non-exo-anomericones, in fast exchange. Very probably, this feature allows the adaptation of these ligands to the spatialand electronic requirements of different receptors. The large diversity of structures adopted by aminoglycosidesin the binding pocket of the different RNA receptors and the distinct enzymes involved in bacterial resistanceare consistent with this view. This conformational diversity can, in certain favorable cases, be exploitedin the design of new antibiotic derivatives not susceptible to enzymatic inactivation, by designing tailor-madeconformationally locked aminoglycosides.

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Correspondence to Juan Luis Asensio or Jesús Jiménez-Barbero .

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Thomas Peters

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© 2007 Springer-Verlag Berlin Heidelberg

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Asensio, J.L., Bastida, A., Jiménez-Barbero, J. (2007). Studies on the Conformational Features of Neomycin-B and its Molecular Recognition by RNA and Bacterial Defense Proteins. In: Peters, T. (eds) Bioactive Conformation II. Topics in Current Chemistry, vol 273. Springer, Berlin, Heidelberg. https://doi.org/10.1007/128_2007_145

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