Proteome-Wide Binding Affinity Profiling.

Authors

Noah Yardeny, Jacob B Geri

Published in

Annual review of pharmacology and toxicology. Jul 06, 2026. Epub Jul 06, 2026.

Abstract

Selective interactions between ligands and protein targets are fundamental to normal biological processes and drug action, and the strength of these interactions is a key metric that defines their functions and disease relevance. Recently introduced methods couple ligand-protein interactions to mass spectrometry-proteomic readouts, enabling the measurement of proteome-wide binding affinity profiles. Here, we review the state of affinity profiling technology, focusing on three key approaches: (a) protein stability-based methods, which detect ligand-induced stabilization against thermal or chemical denaturation; (b) proteolytic resistance-based methods, which infer protein binding through altered susceptibility to enzymatic digestion; and (c) methods that use derivatized probes to capture and enrich ligand-protein complexes.

PMID:
42407117
Bibliographic data and abstract were imported from PubMed on 07 Jul 2026.

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