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Related Experiment Video

Updated: Apr 15, 2026

Deacetylation Assays to Unravel the Interplay between Sirtuins SIRT2 and Specific Protein-substrates
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A FRET-based assay for screening SIRT5 specific modulators.

Yan Li1, Wenfei Huang2, Ling You2

  • 1College of Basic Medical Science, Guiyang Medical University, Guiyang, Guizhou 550004, China.

Bioorganic & Medicinal Chemistry Letters
|March 31, 2015
PubMed
Summary

A new FRET-based assay reliably screens SIRT5 modulators, overcoming false positives from older fluorogenic peptide methods. This breakthrough aids high-throughput drug discovery for SIRT5 targets.

Keywords:
DeacetylationDesuccinylationFRET assayFluorogenic assaySirtuin

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Area of Science:

  • Biochemistry
  • Enzymology
  • Drug Discovery

Background:

  • Sirtuin 5 (SIRT5) functions as a demalonylase and desuccinylase.
  • Existing fluorogenic assays for SIRT5 modulators utilize 7-amino-4-methylcoumarin (AMC), leading to false positive screening results.

Purpose of the Study:

  • To develop a novel, reliable assay for screening small molecule modulators of SIRT5.
  • To overcome the limitations of existing AMC-based assays, specifically false positives.

Main Methods:

  • Development of a Förster Resonance Energy Transfer (FRET)-based assay for SIRT5 activity.
  • Utilizing a substrate devoid of the 7-amino-4-methylcoumarin (AMC) moiety.

Main Results:

  • The FRET-based assay provides a reliable method for assessing SIRT5 activity.
  • This assay effectively eliminates false positive hits associated with AMC.

Conclusions:

  • The developed FRET assay is a robust and accurate tool for high-throughput screening of SIRT5 modulators.
  • This new method enhances the efficiency and reliability of identifying potential therapeutic compounds targeting SIRT5.