STD NMR as a Technique for Ligand Screening and Structural Studies

Abstract

STD NMR is a powerful ligand-based tool for screening small molecules and low molecular weight fragments for their interaction with a given macromolecule. Such information is invaluable both in the drug discovery sector and in understanding fundamental biological interactions. Recently, powerful methods have been developed to extract a greater wealth of information from the STD NMR experiment, including ligand binding epitopes, dissociation constant determination, and mapping of binding site properties. Herein we describe these STD NMR experiments, giving practical examples for each approach, and highlight the important parameters and common pitfalls that must be considered for a successful experiment.

Keywords: Binding epitope mapping; DEEP-STD NMR; Ligand screening; Protein–ligand interactions; STD NMR; Saturation transfer difference NMR.