Virus-ligand interactions: Identification and characterization of ligand binding by NMR spectroscopy

Andrew J. Benie, Rosita Moser, Englbert Bäuml, Dieter Blaas, Thomas Peters*

*Corresponding author for this work
76 Citations (Scopus)


We demonstrate the detection and characterization of ligand binding to viruses via NMR. To illustrate the methodology, the interaction of an antiviral compound with human rhinovirus serotype 2 (HRV2) was investigated. Specific interaction of a capsid-binding inhibitor and native HRV2 was monitored utilizing saturation transfer difference (STD) NMR. STD NMR experiments at atomic resolution allowed those regions of the ligand that are involved in the interaction with the virus to be determined. The approach allows for (i) the fast and robust assessment of binding, (ii) the determination of the ligand binding epitope at atomic resolution without the necessity to crystallize virus-ligand complexes, and (iii) the reuse of the virus in subsequent assays. This methodology enables one to easily identify binding of drugs, peptides, and receptor or antibody fragments to the viral capsid.

Original languageEnglish
JournalJournal of the American Chemical Society
Issue number1
Pages (from-to)14-15
Number of pages2
Publication statusPublished - 08.01.2003

Research Areas and Centers

  • Academic Focus: Center for Infection and Inflammation Research (ZIEL)


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