A New Assay Based on Fluorescence Resonance Energy Transfer to Determine the Binding Affinity of Bcl-x<sub>L</sub>Inhibitors

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  • FENG Yu
    Department of Molecular Pharmacology, Shanghai Institute of Materia Medica, Chinese Academy of Sciences
  • SHEN Xu
    Department of Molecular Pharmacology, Shanghai Institute of Materia Medica, Chinese Academy of Sciences School of Pharmacy, East China University of Science and Technology
  • CHEN Kaixian
    Center for Drug Design and Discovery, State Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences
  • JIANG Hualiang
    Center for Drug Design and Discovery, State Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences School of Pharmacy, East China University of Science and Technology
  • LIU Dongxiang
    Department of Molecular Pharmacology, Shanghai Institute of Materia Medica, Chinese Academy of Sciences

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

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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.

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