Development and optimization of a binding assay for histone deacetylase 4 using surface plasmon resonance

Histone deacetylase 4 (HDAC4) is a histone deacetylase profoundly involved in cell differentiation and in the pathogenesis of cancer. The histone deacetylase inhibitors are a new, promising class of anticancer agents. The screening of molecular interactions involving determination of the affinity of...

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Bibliographic Details
Published in:Analytical biochemistry 2008-06, Vol.377 (2), p.267-269
Main Authors: Mattu, Marco, Di Giovine, Paolo, Steinkuhler, Christian, De Francesco, Raffaele, Altamura, Sergio, Cecchetti, Ottavia, Carfì, Andrea, Barbato, Gaetano
Format: Article
Language:English
Subjects:
Dose-Response Relationship, Drug
Enzyme Inhibitors - metabolism
Enzyme Inhibitors - pharmacology
Enzymes, Immobilized - antagonists & inhibitors
Enzymes, Immobilized - metabolism
Histone Deacetylase Inhibitors
Histone Deacetylases - metabolism
Ketones - chemistry
Ketones - metabolism
Protein Binding
Recombinant Proteins - antagonists & inhibitors
Recombinant Proteins - metabolism
Surface Plasmon Resonance
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Summary:Histone deacetylase 4 (HDAC4) is a histone deacetylase profoundly involved in cell differentiation and in the pathogenesis of cancer. The histone deacetylase inhibitors are a new, promising class of anticancer agents. The screening of molecular interactions involving determination of the affinity of drug candidates is an integral part of the drug discovery process. Here we report the development of an assay using surface plasmon resonance for the analysis of HDAC4–small molecule interactions. We describe a new cloning and purification strategy that can be used to set up surface plasmon resonance experiments with other recombinant proteins.
ISSN:0003-2697
1096-0309
DOI:10.1016/j.ab.2008.03.028