Programme : Back to Mr François Degorce
Poster
31

How do HTRF® epigenetic binding domain assays perform compared to other technologies ?

Discussion

In the past years, significant drug discovery efforts have been made to identify potent and selective inhibitors of epigenetic targets. These proteins have been classified into readers, writers and erasers of various marks affecting histone, other nuclear proteins, and DNA. By regulating a combination of posttranslational marks and through their association with other proteins of the transcription machinery, they tightly control gene expression. Their dysregulation has been linked to the development of broad variety of diseases in oncology, CNS or metabolism.

Binding domains are capable of reading these modifications and act directly on transcription, and they are therefore considered as critical drug targets. In order to help the discovery and the characterization of novel reader domain inhibitors, we have optimized a suite of biochemical assays based on HTRF technology. Using this new platform, more than 25 different assays have been built up to monitor the interaction of Bromodomain, and the BET sub-family. In addition, Tudor domains, MBT domains and chromodomains were assessed the same way with histone peptides. This platform supplements existing HTRF assays enabling the investigation of other important epigenetic targets such as methyltransferases, demethylases, or deacetylases.

In this study, the performance of an HTRF binding domain assay was comprehensively benchmarked against different other commercially available assays, such as Cayman Chemical TR-FRET assay and AlphaScreen technology based assays. This poster provides comparative data on BRD4(1) bromodomain.

Thomas Roux, Najim Douayry, Laurent Sergeant, François Degorce and Eric Trinquet.
Cisbio Bioassays, BP84175, Parc Marcel Boiteux, 30200 Codolet
Programme
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