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Updated: Mar 27, 2026

Deacetylation Assays to Unravel the Interplay between Sirtuins SIRT2 and Specific Protein-substrates

Deacetylation Assays to Unravel the Interplay between Sirtuins SIRT2 and Specific Protein-substrates

Published on: February 27, 2016

Structure-Based Development of an Affinity Probe for Sirtuin 2.

Matthias Schiedel¹, Tobias Rumpf¹, Berin Karaman²

¹Institut für Pharmazeutische Wissenschaften, Albert-Ludwigs-Universität Freiburg, Albertstrasse 25, 79104, Freiburg im Breisgau, Germany.

Angewandte Chemie (International Ed. in English)

|January 11, 2016

Summary

This summary is machine-generated.

Researchers developed a novel Sirt2-selective affinity probe using an optimized sirtuin rearranging ligand (SirReal). This tool aids in studying Sirt2

Keywords:

deacylases drug design protein modifications proteomics sirtuins

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Area of Science:

Biochemistry
Molecular Biology
Drug Discovery

Background:

Sirtuins, specifically Sirt2, are NAD(+)-dependent protein deacylases involved in cellular processes.
Dysregulated Sirt2 activity is linked to cancer, inflammation, and neurodegeneration, highlighting its therapeutic potential.

Purpose of the Study:

To develop the first Sirt2-selective affinity probe.
To utilize a crystal structure of Sirt2 with an optimized sirtuin rearranging ligand (SirReal) for probe development.
To create a tool for studying sirtuin biology and exploring pharmaceutical interventions.

Main Methods:

Crystal structure analysis of Sirt2 in complex with an optimized SirReal ligand.
Development of a Sirt2-selective affinity probe based on the SirReal structure.
Characterization of probe properties including potency, solubility, and cellular efficacy.

Main Results:

The developed SirReal probe exhibits high selectivity for Sirt2.
The probe demonstrates improved potency, water solubility, and cellular efficacy.
A slow dissociation rate of the probe/enzyme complex was observed, enabling new applications.

Conclusions:

The SirReal probe is a valuable tool for biophysical characterization, fragment-based screening, and affinity pull-down assays.
This probe facilitates further research into sirtuin biology and the development of Sirt2-targeted therapies.
The findings open new avenues for drug discovery targeting Sirt2-related diseases.