PMC:7594251 / 47967-49360 JSONTXT

{"target":"https://pubannotation.org/docs/sourcedb/PMC/sourceid/7594251","sourcedb":"PMC","sourceid":"7594251","source_url":"https://www.ncbi.nlm.nih.gov/pmc/7594251","text":"With the pressing search for new antiviral drugs, any techniques for identifying and characterizing novel leads has become increasingly important. Benie et al. [265] described the use of saturation transfer difference (STD) NMR spectroscopy [262,266,267,268,269,270,271] to identify and characterize the binding of an antiviral compound to native human rhinovirus serotype 2 (HRV2). The experiments demonstrated that it is possible to subject targets of the size and complexity of whole viruses (for a model of an HRV2 particle cut open, cf. the table of contents) to STD NMR experiments. The principles of STD NMR have been known for many years [267,268] but it was only recently that the potential of this technique for screening libraries for compounds with binding activity toward protein receptors has been realized [262,266]. The technique also permitted the analysis of epitopes of ligands bound to receptor proteins. Previous NMR studies of virus-ligand interactions used chemical shift titrations, which required very large quantities of the virus. This approach was unworkable when studying pathogenic viruses. Benie et al. [265] demonstrated that solution state STD methodology not only reduces the amount of virus required by approximately 2 orders of magnitude, but also allows for the identification and characterization of virus-ligand interactions with atomic resolution 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