Investigation of labile protein-ligand interactions by native electrospray ionization mass spectrometry

The investigations of noncovalent interaction between proteins (P) and small ligands (L) have played an important role for drug discovery and therapy. Electrospray ionization mass spectrometry (ESI-MS) has been typically applied to analysis of P-L interactions. However, some labile complexes are problematic for determination of association constants (Ka) by ESI-MS due to their in-source dissociation. Here, a strategy based on native MS for...