We have developed the STD NMR protocol to elucidate ligand-receptor interactions by NMR. We can characterize the binding epitope of the ligands to the receptor and can achieve a very high sensitivity in terms of amount of protein required. We can also determine KD values and association and dissociation kinetics (koff and kon).The receptor can be any type of protein either being soluble or even membrane integrated. Even proteins on the surface of native whole cells can be analyzed. At the minimum, the need for protein is down to about 30 picomols of protein to obtain an STD NMR spectrum.
Direct observation of ligand binding to membrane proteins in living cells by STDD NMR,
Birgit Claasen, Marko Axmann, Robert Meinecke & Bernd Meyer,
J. Am. Chem. Soc. 127, 916-919 (2005).
Group Epitope Mapping (GEM) by STD NMR to Identify Segments of a Ligand in Direct Contact with a Protein Receptor.
Moriz Mayer and Bernd Meyer,
J. Am. Chem. Soc. 123, 6108-6117 (2001).
Detecting Binding Affinity to Immobilized Receptor Proteins in Compound Libraries by HR-MAS STD NMR,
Jens Klein, Robert Meinecke, Moriz Mayer & Bernd Meyer,
J. Am. Chem. Soc. 121, 5336-5337 (1999).
A Fast and Sensitive Method to Characterize Ligand Binding by Saturation Transfer Difference NMR Spectra,
M. Mayer & B. Meyer,
Angew. Chem. Int. Ed. 38, 1784-1788 (1999); Angew. Chem. 111, 1902-1906 (1999).
Analysis of Specificity and Epitope of Ganglioside Oligosaccharides Binding to Myelin Associated Glycoprotein (MAG) by Saturation Transfer Difference NMR,
So-Young Shin, Heiko Gäthje, Oliver Schwardt, Beat Ernst, Soerge Kelm and Bernd Meyer,
ChemBioChem 9, 2946 – 2949 (2008).