FP tethering: a screening technique to rapidly identify compounds that disrupt protein-protein interactions
FP tethering: a screening technique to rapidly identify compounds that disrupt protein-protein interactions
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DOI:
10.1039/c3md00356f
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发表时间:
2014-03-01
期刊:
影响因子:
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通讯作者:
Mapp, Anna K.
中科院分区:
文献类型:
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作者:
Lodge, Jean M.;Rettenmaier, T. Justin;Mapp, Anna K.
Tethering is a screening technique for discovering small-molecule fragments that bind to pre-determined sites via formation of a disulphide bond. Tethering screens traditionally rely upon mass spectrometry to detect disulphide bond formation, which requires a time-consuming liquid chromatography step. Here we show that tethering can be performed rapidly and inexpensively using a homogenous fluorescence polarization (FP) assay that detects displacement of a peptide ligand from the protein target as an indirect readout of disulphide formation. We apply this method, termed FP tethering, to identify fragments that disrupt the protein-protein interaction between the KIX domain of the transcriptional coactivator CBP and the transcriptional activator peptide pKID.