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Förster resonance energy transfer-based cholesterolysis assay identifies a novel hedgehog inhibitor
- Source :
- Analytical Biochemistry. 488:1-5
- Publication Year :
- 2015
- Publisher :
- Elsevier BV, 2015.
-
Abstract
- Hedgehog (Hh) proteins function in cell/cell signaling processes linked to human embryo development and the progression of several types of cancer. Here, we describe an optical assay of hedgehog cholesterolysis, a unique autoprocessing event critical for Hh function. The assay uses a recombinant Förster resonance energy transfer (FRET)-active Hh precursor whose cholesterolysis can be monitored continuously in multi-well plates (dynamic range=4, Z'=0.7), offering advantages in throughput over conventional sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) assays. Application of the optical assay in a pilot small molecule screen produced a novel cholesterolysis inhibitor (apparent IC50=5×10(-6)M) that appears to inactivate hedgehog covalently by a substitution nucleophilic aromatic (SNAr) mechanism.
- Subjects :
- Cell signaling
Recombinant Fusion Proteins
Amino Acid Motifs
Biophysics
Tetrazoles
Antineoplastic Agents
Pilot Projects
Biochemistry
Article
Small Molecule Libraries
Nucleophilic aromatic substitution
Fluorescence Resonance Energy Transfer
Animals
Drosophila Proteins
Point Mutation
Hedgehog Proteins
Protein Interaction Domains and Motifs
Protein Precursors
Molecular Biology
Hedgehog
Conserved Sequence
Gel electrophoresis
Chemistry
Cell Biology
Protein engineering
Small molecule
Peptide Fragments
Hedgehog signaling pathway
High-Throughput Screening Assays
Kinetics
Luminescent Proteins
Cholesterol
Drosophila melanogaster
Förster resonance energy transfer
Nitrobenzoates
Proteolysis
Protein Processing, Post-Translational
Subjects
Details
- ISSN :
- 00032697
- Volume :
- 488
- Database :
- OpenAIRE
- Journal :
- Analytical Biochemistry
- Accession number :
- edsair.doi.dedup.....41e5667e7e37ed11206b2bd35ec73b16