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Bromodomains, which read acetylated lysine marks, can form amyloid-like aggregates. Inhibitors targeting CBP/p300 bromodomains reduce this protein aggregation and HDAC inhibitor-induced cytotoxicity.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Epigenetics

Background:

  • Bromodomains are epigenetic readers recognizing acetylated lysine residues.
  • These domains are crucial for regulating gene transcription and DNA repair.
  • CBP/p300 are key epigenetic regulators containing bromodomains.

Purpose of the Study:

  • To investigate the role of CBP/p300 bromodomains in protein aggregation.
  • To determine if CBP/p300 bromodomain inhibitors can prevent amyloid-like aggregate formation.
  • To assess the impact of these inhibitors on histone deacetylase (HDAC) inhibitor-induced cytotoxicity.

Main Methods:

  • Biochemical assays to detect protein aggregation.
  • Structural analysis of bromodomain-mediated aggregate formation.
  • In vitro and in vivo studies using specific bromodomain inhibitors.
  • Cell-based assays to measure cytotoxicity.

Main Results:

  • CBP/p300 bromodomains were found to mediate the formation of amyloid-like protein aggregates.
  • Specific inhibitors targeting CBP/p300 bromodomains significantly reduced protein aggregation.
  • These inhibitors also mitigated cytotoxicity induced by HDAC inhibitors.

Conclusions:

  • CBP/p300 bromodomains are implicated in amyloid-like aggregate formation.
  • Targeting these bromodomains with inhibitors offers a potential therapeutic strategy.
  • Bromodomain inhibition may overcome resistance or reduce side effects associated with epigenetic therapies.