A novel cholesterol‐based detergent

Design, synthesis and characterization of CHAPSTEROL, a novel cholesterol‐based detergent developed for functional solubilization of cholesterol‐dependent membrane proteins are described. To validate CHAPSTEROL, we employed the oxytocin receptor, a G protein‐coupled receptor requiring cholesterol fo...

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Bibliographic Details
Published in:The FEBS journal 2005-02, Vol.272 (3), p.800-812
Main Authors: Gehrig‐Burger, Katja, Kohout, Ladislav, Gimpl, Gerald
Format: Article
Language:English
Subjects:
CHAPSTEROL
detergent
photoreactive cholesterol
rafts
steroid nucleus
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Summary:Design, synthesis and characterization of CHAPSTEROL, a novel cholesterol‐based detergent developed for functional solubilization of cholesterol‐dependent membrane proteins are described. To validate CHAPSTEROL, we employed the oxytocin receptor, a G protein‐coupled receptor requiring cholesterol for its high‐affinity binding state. Using the photoactivatable cholesterol analogue [3H]6,6‐azocholestan‐3β‐ol[3αH], we demonstrate that solubilization by CHAPSTEROL leads to an enrichment of cholesterol‐binding proteins whereas the widely used bile acid derivative CHAPSO leads to a significant depletion of cholesterol‐binding proteins. Similar to Triton X‐100 and CHAPS, CHAPSTEROL maintains the localization of caveolin as well as cholesterol and sphingomyelin to lipid rafts, i.e. detergent‐insoluble microdomains of the plasma membrane. The data suggest that CHAPSTEROL is an appropriate detergent for the solubilization of cholesterol‐dependent membrane proteins and isolation of rafts.
ISSN:1742-464X
1742-4658
DOI:10.1111/j.1742-4658.2004.04517.x