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Simultaneous Measurement of HDAC1 and HDAC6 Activity in HeLa Cells Using UHPLC-MS
Published on: August 10, 2017
Fluorescence-labeled octapeptides as substrates for histone deacetylase
K Hoffmann1, R M Söll, A G Beck-Sickinger
1Department of Pharmaceutical Chemistry, Westfälische Wilhelms-Universität Münster, Hittorfstrasse 58-62, 48149 Münster, Germany.
Bioconjugate Chemistry
|February 15, 2001
Summary
Researchers developed fluorescein-labeled octapeptides to assay histone deacetylase (HDAC) activity. This method offers a more accurate way to screen for HDAC inhibitors, crucial for cancer cell differentiation and apoptosis.
Area of Science:
- Biochemistry
- Molecular Biology
- Enzymology
Background:
- Histone deacetylases (HDACs) regulate gene transcription.
- HDAC inhibitors can induce cancer cell differentiation and apoptosis.
- Accurate assays for HDAC activity are vital for drug screening.
Purpose of the Study:
- To develop novel substrates for histone deacetylase (HDAC) activity determination.
- To evaluate fluorescein-labeled octapeptides as substrates for HDAC assays.
- To establish a method for analyzing HDAC deacetylation kinetics and site selectivity.
Main Methods:
- Synthesis of fluorescein-labeled octapeptides as potential HDAC substrates.
- High-Performance Liquid Chromatography (HPLC) with fluorescence detection for deacetylation analysis.
- Liquid Chromatography-Mass Spectrometry (LC-MS) for result confirmation.
Main Results:
- Fluorescein-labeled octapeptides serve as effective substrates for HDACs.
- HPLC-fluorescence detection accurately quantifies time- and site-dependent deacetylation.
- LC-MS confirmed deacetylation findings, showing potential site selectivity.
Conclusions:
- Fluorescein-labeled octapeptides provide a valuable tool for HDAC activity assays.
- The developed methodology can be extended to larger peptides for detailed HDAC characterization.
- This approach aids in the development of targeted HDAC inhibitors for cancer therapy.
