Chapter title |
Using AlphaScreen(®) to Identify Small-Molecule Inhibitors Targeting a Conserved Host-Pathogen Interaction.
|
---|---|
Chapter number | 30 |
Book title |
Proteostasis
|
Published in |
Methods in molecular biology, January 2016
|
DOI | 10.1007/978-1-4939-3756-1_30 |
Pubmed ID | |
Book ISBNs |
978-1-4939-3754-7, 978-1-4939-3756-1
|
Authors |
Sisley Austin, Saïd Taouji, Eric Chevet, Harald Wodrich, Fabienne Rayne |
Editors |
Rune Matthiesen |
Abstract |
AlphaScreen(®) is a technology particularly suitable for bi-molecular inhibitor screening assays, e.g. using protein-protein interactions with purified recombinant proteins. Each binding partner of the bi-molecular interaction is coupled either to donor or to acceptor beads. The technology is based on the quantifiable transfer of oxygen singlets from donor to acceptor microbeads brought together by a specific interaction between the partners. We identified the conserved interaction between WW domains of cellular ubiquitin ligases of the Nedd4 family and a short peptide motif (PPxY) present in several structural and non-structural viral proteins as a potential drug target. Using an AlphaScreen assay recapitulating the interaction between Nedd4.2 and the PPxY motif of the adenoviral capsid protein VI, we screened a library of small molecules and identified specific inhibitors of this interaction. |
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