Related Experiment Video
Updated: Apr 28, 2026

Deacetylation Assays to Unravel the Interplay between Sirtuins SIRT2 and Specific Protein-substrates
Published on: February 27, 2016
A High-throughput Fluorescence Polarization Assay for Screening Sirtuin Inhibitors
Kewen Peng1,2, Suryadeep Chakraborty1,3, Yizhen Jin1,3
1Department of Medicine, The University of Chicago, Chicago, IL 60637, USA.
Researchers developed a new assay for screening sirtuin inhibitors, crucial for cancer drug development. This high-throughput method uses less enzyme, accelerating the discovery of potential anticancer therapeutics targeting sirtuins (SIRTs).
Area of Science:
- Biochemistry
- Molecular Biology
- Drug Discovery
Background:
- Sirtuins (SIRTs) are enzymes that remove protein lysine acyl modifications, regulating vital cellular processes like metabolism, gene transcription, DNA repair, and stress response.
- Several SIRTs are implicated in cancer as non-oncogene addiction targets, making them promising candidates for anticancer drug development.
- Developing potent and isoform-selective SIRT inhibitors requires effective high-throughput screening (HTS) methods.
Purpose of the Study:
- To design and synthesize a novel fluorescent polarization (FP) tracer for sirtuin activity.
- To develop a robust, high-throughput FP competition assay for screening inhibitors of SIRT1-3.
- To validate the assay's performance and demonstrate its utility in accelerating SIRT inhibitor discovery.
Main Methods:
- Design and synthesis of a high-affinity fluorescent polarization (FP) tracer, KP-SC-1.
- Development of a high-throughput FP competition assay for SIRT1-3 inhibition screening.
- Validation of the assay using known SIRT1-3 inhibitors and assessment of its stability and performance in pilot library screening.
Main Results:
- A novel FP tracer, KP-SC-1, was successfully synthesized and utilized to establish a robust HTS assay for SIRT1-3.
- The assay demonstrated effectiveness in detecting both NAD+-dependent and NAD+-independent SIRT1-3 inhibitors.
- The developed FP assay requires significantly less SIRT1-3 enzyme compared to previous methods, enhancing its suitability for large-scale screening.
Conclusions:
- The newly developed FP competition assay is a stable and high-performing method for screening SIRT1-3 inhibitors.
- This assay's reduced enzyme requirement makes it particularly advantageous for high-throughput library screening.
- The assay is expected to accelerate the discovery and development of novel SIRT1-3 inhibitors for potential therapeutic applications, especially in cancer.
More Related Videos
07:37Click-Chemistry Based Fluorometric Assay for Apolipoprotein N-acyltransferase from Enzyme Characterization to High-Throughput Screening
Published on: May 13, 2020
05:46Fluorescence-Based Detection of FEN1 Nuclease Activity and Screening of Small-Molecule Inhibitors
Published on: June 27, 2025