https://doi.org/10.15255/KUI.2007.006
Published: Kem. Ind. 57 (4) (2008) 165–173
Paper reference number: KUI-06/2007
Paper type: Review
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Ligand-receptor Interactions by NMR Spectroscopy

P. Tepeš and P. Novak

Abstract

Today NMR spectroscopy is a method of choice for elucidation of interactions between biomolecules and the potential ligands. Knowledge on these interactions is an essential prerequisite for the rational drug design. The most important contribution of NMR to drug design a few years ago was the 3D structure determination of proteins. Besides delivering the 3D structures of the free proteins as a raw material for the modeling studies on ligand binding, NMR can directly yield valuable experimental data on the biologically important protein-ligand complexes. In addition to X- -ray diffraction, NMR spectroscopy can provide information on the internal protein dynamics or dynamics of intermolecular interactions. Changes in NMR parameters allow us to detect (“SAR by NMR”) and quantitatively determine binding affinities (titration, diffusion NMR experiments, etc.) of potential ligands. Also, it is possible to determine the binding site and conformations of ligands, receptors and receptor-ligand complexes with the help of NMR methods such as tr-NOESY. Epitopes or functional groups responsible for binding of ligands to the receptor can be identified by employing STD or WaterLOGSY experiments. In this review are described some of the most frequent NMR methods for the characterization of the interactions between biomolecules and ligands, together with their advantages and disadvantages.

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Keywords

nuclear magnetic resonance, receptor, ligand, complex receptor-ligand, NMR parameters, structure, binding affinity, active site, dissociation constant, diffusion, NOE, epitopes