Histone Acetyltransferase Enzymes: From Biological Implications to Most Relevant Inhibitors

Daniela Trisciuoglio, Dante Rotili

Research output: Chapter in Book/Report/Conference proceedingChapter


The acetylation of lysine residues of histone and nonhistone proteins is a post-translational modification catalysed by the so-called histone acetyltransferases (HATs) that plays a crucial role in several biological settings. The deregulation of this enzymatic activity is implicated in many disease conditions such as cancer and inflammatory and neurological disorders. Despite many histone acetyltransferase inhibitors (HATi) have been identified so far, there is still the need for new, metabolically stable, more potent and selective HATi as potential therapeutic agents and/or as chemical tools for studying HAT biology. In the present chapter, the main features of HAT enzymes and related diseases have been summarized, with a particular focus on HATi, analysing their structure-activity relationships, mechanisms of action and potential therapeutic applications.

Original languageEnglish
Title of host publicationTopics in Medicinal Chemistry
Number of pages30
Publication statusPublished - 2020

Publication series

NameTopics in Medicinal Chemistry
ISSN (Print)1862-2461
ISSN (Electronic)1862-247X


  • Cancer
  • Chemical probes
  • Epigenetics
  • Histone acetyltransferase inhibitors
  • Structure- and ligand-based drug discovery

ASJC Scopus subject areas

  • Molecular Medicine
  • Drug Discovery


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