Recursos - Pôsteres Científicos
Screening for Inhibitors of BRD4 Bromodomain 1 using a Homogeneous Proximity AssayDownload
Related Products: Synergy Neo2
January 14, 2013
Authors: P. Brescia, B. Larson and P. Banks, BioTek Instruments, Inc., Winooski, Vermont; D. Bochar and L. Blazer, Cayman Chemical Co., Ann Arbor, Michigan
Bromodomains recognize acetylated lysine residues of histones and facilitate recruitment of protein complexes as part of the epigenetic regulation of gene transcription. The BET family of proteins, which contain tandem repeats of Bromodomains plus an Extra Terminal domain, play a role in bridging acetylation and transcriptional regulation of diverse cellular processes such as inflammatory gene expression, mitosis and viral/host interactions. Several small molecule inhibitors have been identified that disrupt bromodomain/acetylated lysine interactions. Here we demonstrate the automation of a homogeneous, TR-FRET (Time-Resolved Fluorescence Resonance Energy Transfer) assay method suitable for high throughput screening and rapid characterization of inhibitors of bromodomain/acetylated peptide interactions. Demonstration of the assay includes a screen of a small library of natural products under primary screening conditions against the BRD4 bromodomain 1 (human amino acids 49-170).