Quantitative Characterization of Three Carbonic Anhydrase Inhibitors by LESA Mass Spectrometry.

ABSTRACT: Liquid extraction surface analysis (LESA) coupled to native mass spectrometry (MS) presents unique analytical opportunities due to its sensitivity, speed, and automation. Here, we examine whether this tool can be used to quantitatively probe protein-ligand interactions through calculation of equilibrium dissociation constants (K_d values). We performed native LESA MS analyses for a well-characterized system comprising bovine carbonic anhydrase II and the ligands chlorothiazide, dansylamide, and sulfanilamide, and compared the results with those obtained from direct infusion mass spectrometry and surface plasmon resonance measurements. Two LESA approaches were considered: In one approach, the protein and ligand were premixed in solution before being deposited and dried onto

SUBMITTER: Illes-Toth E 

PROVIDER: S-EPMC9264382 | biostudies-literature | 2022 Jul

REPOSITORIES: biostudies-literature