Related Experiment Video
Updated: Aug 26, 2025

Deacetylation Assays to Unravel the Interplay between Sirtuins SIRT2 and Specific Protein-substrates
Published on: February 27, 2016
Discovery of novel compounds as potent activators of Sirt3
Célina Reverdy1, Gaetan Gitton1, Xiangying Guan2
1Center for Protein Engineering & Drug Discovery, PMC Isochem SAS, 32 rue Lavoisier, F-91710 Vert-le-Petit, France.
Abstract:
Among the sirtuin enzymes, Sirt3 is one of the most important deacetylases as it regulates acetylation levels in mitochondria, which are linked to the metabolism of multiple organs and therefore involved in many types of age-related human diseases such as cancer, heart diseases and metabolic diseases. Given the dearth of direct activators of Sirt3, the identification of new modulators could be a key step in the development of new therapeutics. Here we report the discovery of Sirt3 modulators, including activators, through the use of DNA encoded library technology (DEL) and computational high-throughput screening methodologies. Top hits from both screenings against Sirt3 were evaluated according to their activity and affinity. Our best activator is more potent than the previously reported activator Honokiol. Docking studies suggest that our activators identified from virtual screening interact with Sirt3 at a site similar to Honokiol, whereas the activators identified from DEL selection interact with Sirt3 at an atypical site. Our results establish the attractiveness of these high-throughput screening technologies in identifying novel and potent Sirt3 activators and, therefore, in associated therapeutic applications.
More Related Videos
10:25Screening Traditional Chinese Medicine Compounds for Inhibiting UCHL3 Activity Based on Molecular Docking and Deubiquitinating Enzyme Probe Technology
Published on: November 22, 2024
10:21Author Spotlight: Streamlining Protein Target Prediction and Validation via Molecular Docking and CETSA
Published on: February 23, 2024