Histone deacetylases (HDACs) are validated targets for treatment of certain cancer types and play numerous regulatory roles in biology, ranging from epigenetics to metabolism. Small molecules are highly important as tool compounds to probe these mechanisms as well as for the development of new medicines. Therefore, detailed mechanistic information and precise characterization of the enzyme
substrate preference as well as development of chemical probes to investigate the effects of HDAC enzymes are vital. Through profiling of both sirtuins and zincdependent HDACs, we have developed
efficient assay formats for inhibitor characterization and discovered enzymatic activities against novel ε-N-acyllysine posttranslational modifications, most recently εN-lactyllysine. In this presentation, I will focus on our advances in the selective targeting of SIRT5, SIRT7 and HDAC11, using different strategies
including covalent targeting and macrocyclic peptide inhibitors.
15/07/2025
Aula A, CU018, 16.00