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A non-isotopic assay for histone deacetylase activity
K Hoffmann1, G Brosch, P Loidl
1Department of Pharmaceutical Chemistry, Westfälische Wilhelms-Universität Münster, Hittorfstrasse 58-62,48149 Münster, Germany.
Nucleic Acids Research
|April 13, 1999
Summary
Histone deacetylase (HD) inhibitors show promise for cancer treatment. A new, non-radioactive assay enables efficient screening of potential HD inhibitors for drug discovery and purification.
Area of Science:
- Biochemistry
- Molecular Biology
- Drug Discovery
Background:
- Histone deacetylase (HD) inhibitors are promising cancer therapeutics.
- Existing in vitro assays for HD activity and inhibition are often radioactive.
Purpose of the Study:
- To develop a simple, non-radioactive assay for screening histone deacetylase (HD) inhibitors.
- To facilitate the identification and purification of HD enzymes.
Main Methods:
- Established a novel assay using an aminocoumarin derivative of omega-acetylated lysine as a substrate.
- The assay is designed for high-throughput screening of numerous compounds.
Main Results:
- Successfully developed a simple, non-radioactive assay for HD activity.
- The assay allows for the screening of a large number of potential HD inhibitors.
Conclusions:
- The new assay provides a valuable tool for identifying and purifying histone deacetylase (HD) enzymes.
- This non-radioactive method is suitable for large-scale screening in drug discovery efforts.