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Förster resonance energy transfer-based cholesterolysis assay identifies a novel hedgehog inhibitor

Authors :
George Ngoje
Travis J. Lageman
Marlene Belfort
Brian P. Callahan
Brandon M. Bordeau
Timothy S. Owen
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.

Details

ISSN :
00032697
Volume :
488
Database :
OpenAIRE
Journal :
Analytical Biochemistry
Accession number :
edsair.doi.dedup.....41e5667e7e37ed11206b2bd35ec73b16