About event
Saturation Transfer Difference (STD) NMR is a powerful ligand-based NMR technique for weak ligand screening and to gain quantitative structural information from biologically relevant protein-ligand complexes.[1]
The approach is appropriate for small molecule binders of medium-weak affinity (dissociation constant of high nM to low mM), there is no upper limit for protein size, and labeling is not required. The technique is highly versatile and popular in the context of hit identification in drug discovery. In this talk, the investigation by STD NMR of molecular recognition processes of glycans by biologically relevant protein receptors will be presented.[2-5]
Protein-glycan interactions are among the most relevant protein-ligand interactions of weak affinity and high specificity. Nature has evolved to use glycans for controlling many biological or pathological processes like cell-to-cell communication, immunity and inflammation, infection, a progression of cancer.[6]
Along the talk, novel methodological developments in STD NMR will also be presented, describing how the process of fast ligand rebinding can affect the determination of accurate dissociation constants by STD NMR,[7] as well as the development of the method “DiffErential EPitope mapping (DEEP-STD NMR)” [8] that allows identifying the nature of the protein-ligand contacts in the bound state.
Poster to download here.