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Related Experiment Video

Updated: Apr 14, 2026

Deacetylation Assays to Unravel the Interplay between Sirtuins SIRT2 and Specific Protein-substrates
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A FRET-based assay for screening SIRT6 modulators.

Yan Li1, Ling You2, Wenfei Huang2

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

European Journal of Medicinal Chemistry
|April 18, 2015
PubMed
Summary

A new FRET-based assay offers a reliable method for screening SIRT6 modulators, overcoming false positives associated with previous fluorogenic assays for this sirtuin enzyme.

Keywords:
DeacetylationDefatty-acylationFRET assayFluorogenic assaySirtuin

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Area of Science:

  • Biochemistry
  • Enzymology
  • Drug Discovery

Background:

  • Sirtuins, including SIRT6, are implicated in human disease therapeutics.
  • SIRT6 functions as a deacylase, removing long-chain fatty acyl groups.
  • Existing fluorogenic assays for SIRT6 screening are prone to false positives due to the use of 7-amino-4-methylcoumarin (AMC).

Purpose of the Study:

  • To develop a more reliable assay for screening small molecule modulators of SIRT6.
  • To overcome the limitations of existing AMC-based fluorogenic assays.

Main Methods:

  • Development of a Förster Resonance Energy Transfer (FRET)-based assay for SIRT6.
  • Utilizing the FRET assay in a high-throughput screening format.

Main Results:

  • The FRET-based assay provides a reliable method for SIRT6 modulator screening.
  • Elimination of the AMC group prevents false positive hits observed in previous assays.

Conclusions:

  • The developed FRET assay is a valuable tool for high-throughput screening of SIRT6 modulators.
  • This assay offers improved accuracy and reliability for drug discovery efforts targeting SIRT6.