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A New Assay Based on Fluorescence Resonance Energy Transfer to Determine the Binding Affinity of Bcl-xL Inhibitors

We developed a new assay of Bcl-xL inhibitors based on fluorescence resonance energy transfer that occurs between an AEDANS-labeled Bak-BH3 peptide and three tryptophans in the BH1 and BH2 domains of Bcl-xL. The method can tolerate up to 5% DMSO, and it was validated with several Bcl-xL inhibitors. It can be adapted to screen for compounds targeting other Bcl-2 family proteins.