Protein-Ligand Interaction I: STD experiments

Saturation Transfer Difference (STD) NMR spectroscopy is a very useful tool for screening  compounds for protein-binding activity. 1.2) In this method, the magnetization from proteins transfers to all compounds in solution, but only the compound with binding activity will be saturated due to  the protein-ligand interaction. The difference between a saturation transfer difference spectrum and  a normal NMR spectrum can clearly identify binding-activity compounds. Recently we have used  this method on albumin, L-(+)-arginine and L-tryptophan as standard experiments on a JEOL Resonance JNM-ECS 400MHz spectrometer.
Here we show the results of 1D and 2D STD experiments.

Referene

• (1)Moriz Mayer and Bernd Meyer, Angew. Chem. Int. Ed. 1999, 38, 1784-1787.
• (2)Moriz Mayer and Bernd Meyer, J. Am. Chem. Soc. 2001, 123, 6108-6117.