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Bromodomain-containing proteins are epigenetic modulators involved in a wide range of cellular processes, from recruitment of transcription factors to pathological disruption of gene regulation and cancer development. Since the druggability of these acetyl-lysine reader domains was established, efforts were made to develop potent and selective inhibitors across the entire family. Here we report the development of a small molecule-based approach to covalently modify recombinant and endogenous bromodomain-containing proteins by targeting a conserved lysine and a tyrosine residue in the variable ZA or BC loops. Moreover, the addition of a reporter tag allowed in-gel visualization and pull-down of the desired bromodomains.

Original publication

DOI

10.1002/anie.201807825

Type

Journal article

Journal

Angew Chem Int Ed Engl

Publication Date

21/01/2019

Volume

58

Pages

1007 - 1012

Keywords

activity-based protein profiling, bromodomain, chemical proteomics, covalent probes, epigenetics