Disrupting Acetyl-Lysine Recognition: Progress in the Development of Bromodomain Inhibitors

J Med Chem. 2016 Feb 25;59(4):1271-98. doi: 10.1021/acs.jmedchem.5b01514. Epub 2015 Dec 1.

Abstract

Bromodomains, small protein modules that recognize acetylated lysine on histones, play a significant role in the epigenome, where they function as "readers" that ultimately determine the functional outcome of the post-translational modification. Because the initial discovery of selective BET inhibitors have helped define the role of that protein family in oncology and inflammation, BET bromodomains have continued to garner the most attention of any other bromodomain. More recently, non-BET bromodomain inhibitors that are potent and selective have been disclosed for ATAD2, CBP, BRD7/9, BRPF, BRPF/TRIM24, CECR2, SMARCA4, and BAZ2A/B. Such novel inhibitors can be used to probe the physiological function of these non-BET bromodomains and further understanding of their role in certain disease states. Here, we provide an update to the progress in identifying selective bromodomain inhibitors and their use as biological tools, as well as our perspective on the field.

MeSH terms

  • ATPases Associated with Diverse Cellular Activities
  • Acetylation / drug effects*
  • Adaptor Proteins, Signal Transducing / antagonists & inhibitors
  • Adaptor Proteins, Signal Transducing / metabolism
  • Adenosine Triphosphatases / antagonists & inhibitors
  • Adenosine Triphosphatases / metabolism
  • Animals
  • Antigens, Nuclear / metabolism
  • CREB-Binding Protein / antagonists & inhibitors
  • CREB-Binding Protein / metabolism
  • Carrier Proteins / antagonists & inhibitors
  • Carrier Proteins / metabolism
  • Cell Cycle Proteins
  • Chromosomal Proteins, Non-Histone / antagonists & inhibitors
  • Chromosomal Proteins, Non-Histone / metabolism
  • DNA Helicases / antagonists & inhibitors
  • DNA Helicases / metabolism
  • DNA-Binding Proteins / antagonists & inhibitors
  • DNA-Binding Proteins / metabolism
  • Drug Discovery* / methods
  • Histones / metabolism*
  • Humans
  • Lysine / metabolism*
  • Models, Molecular
  • Nerve Tissue Proteins / antagonists & inhibitors
  • Nerve Tissue Proteins / metabolism
  • Nuclear Proteins / antagonists & inhibitors
  • Nuclear Proteins / metabolism
  • Protein Processing, Post-Translational / drug effects*
  • Protein Serine-Threonine Kinases / antagonists & inhibitors
  • Protein Serine-Threonine Kinases / metabolism
  • RNA-Binding Proteins / antagonists & inhibitors
  • RNA-Binding Proteins / metabolism
  • Small Molecule Libraries / chemistry*
  • Small Molecule Libraries / pharmacology*
  • Transcription Factors / antagonists & inhibitors
  • Transcription Factors / metabolism

Substances

  • Adaptor Proteins, Signal Transducing
  • Antigens, Nuclear
  • BAZ2A protein, human
  • BRD2 protein, human
  • BRD3 protein, human
  • BRD4 protein, human
  • BRD7 protein, human
  • BRD9 protein, human
  • BRDT protein, human
  • BRPF1 protein, human
  • Carrier Proteins
  • Cecr2 protein, human
  • Cell Cycle Proteins
  • Chromosomal Proteins, Non-Histone
  • DNA-Binding Proteins
  • Histones
  • Nerve Tissue Proteins
  • Nuclear Proteins
  • RNA-Binding Proteins
  • Small Molecule Libraries
  • TRIM24 protein, human
  • Transcription Factors
  • fetal Alzheimer antigen
  • CREB-Binding Protein
  • CREBBP protein, human
  • Protein Serine-Threonine Kinases
  • Adenosine Triphosphatases
  • SMARCA4 protein, human
  • ATAD2 protein, human
  • ATPases Associated with Diverse Cellular Activities
  • DNA Helicases
  • Lysine