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

Yu FENG; Xu SHEN; Kaixian CHEN; Hualiang JIANG; Dongxiang LIU

doi:10.1271/bbb.70735

This article has now been updated. Please use the final version.

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

Yu FENG, Xu SHEN, Kaixian CHEN, Hualiang JIANG, Dongxiang LIU

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Keywords: fluorescence resonance energy transfer, Bcl-x_L, inhibitor, binding assay, apoptosis

JOURNAL FREE ACCESS Advance online publication

Article ID: 70735

DOI https://doi.org/10.1271/bbb.70735

The final version of this article is now available: Vol. 72 (2008) , No. 7 p.1936

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Abstract

We developed a new assay of Bcl-x_L 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-x_L. The method can tolerate up to 5% DMSO, and it was validated with several Bcl-x_L inhibitors. It can be adapted to screen for compounds targeting other Bcl-2 family proteins.

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