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9. Detection of Noncovalent Protein-Ligand Complexes by IR-MALDESI-MS.

Author

Knizner KT, Pu F, Sawicki JW, Radosevich AJ, Ugrin SA, Elsen NL, Williams JD, and Muddiman DC

Subjects
Ligands, Carbonic Anhydrases chemistry, Carbonic Anhydrases metabolism, Carbonic Anhydrases analysis, Protein Binding, Agammaglobulinaemia Tyrosine Kinase metabolism, Agammaglobulinaemia Tyrosine Kinase chemistry, Agammaglobulinaemia Tyrosine Kinase antagonists & inhibitors, Humans, Proteins chemistry, Proteins metabolism, Proteins analysis, Mass Spectrometry methods
Abstract

Native mass spectrometry (MS) is a powerful analytical technique to directly probe noncovalent protein-protein and protein-ligand interactions. However, not every MS platform can preserve proteins in their native conformation due to high energy deposition from the utilized ionization source. Most small molecules approved as drugs and in development interact with their targets through noncovalent interactions. Therefore, rapid methods to analyze noncovalent protein-ligand interactions are necessary for the early stages of the drug discovery pipeline. Herein, we describe a method for analyzing noncovalent protein-ligand complexes by IR-MALDESI-MS with analysis times of ∼13 s per sample. Carbonic anhydrase and the kinase domain of Bruton's tyrosine kinase are paired with known noncovalent binders to evaluate the effectiveness of native MS by IR-MALDESI.

Published
2024
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