Protein-ligand binding, selectivity, and affinity govern the cellular effects of drugs and endogenous molecules. Current methods typically rely on qualitative omics analysis followed by affinity measurements using purified proteins or engineered reporters. Few approaches enable simultaneous target identification and quantitative affinity measurement, and those are often limited to specific enzyme classes or ligand-induced stability shifts.
We present Affinity Map, a general platform that integrates competitive binding, high-fidelity photocatalytic labeling, and high-throughput proteomics to globally quantify protein-ligand affinities. Affinity Map profiles binding across diverse ligand types—including small molecules, linear and cyclic peptides, and antibodies—directly in complex samples such as cell lysates, organ extracts, and live cell surfaces using unmodified ligands.
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Global Protein-Ligand Binding Affinity Profiling via Photocatalytic Labeling. Charles David Warren, Noah Yardeny, Siyang Peng, Colin Spencer Burdette, Jacob B Geri.
doi: https://doi.org/10.1101/2025.07.04.662444
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