Our review on probing epigenetic reader domains with chemical biology is now published in Current Opinion in Chemical Biology

  • for website
  • Figure 1. Structural architecture of reader domains.
  • Figure 2. Photoaffinity probes and click chemistry approaches.
  • Figure 3. Fragment-based and peptide-based approaches
  • Figure 4. Bivalent ligands of epigenetic readers.
  • Figure 5. PROTAC degraders of epigenetic readers.

Congratulations to Alessandra Cipriano, well done! Alessandra was a visiting PhD student with us, from Gianluca Sbardella's group at the University of Salerno

Read the article here.

Authors: Alessandra Cipriano, Gianluca Sbardella* and Alessio Ciulli*

Title: Targeting epigenetic reader domains by chemical biology


Over the past years, growing interest toward post-translational modifications (PTMs) of histones and nonhistone proteins has prompted academia and industrial research groups to develop different approaches to better understand the link between PTMs and pathological states. Selective recognition of PTMs is carried out by reader modules, which mediate the biological readout of epigenetic mechanisms. Progress in medicinal chemistry and chemical biology has contributed to corroborate the role of reader domains in chromatin-binding proteins as potential therapeutic targets. Here, we review the state-of-the-art of the most important small molecules developed to date, with a particular attention on contemporary chemical biology approaches, including photoaffinity probes, cyclic peptides, bifunctional inhibitors, and PROTAC degraders.