Cholesterol Chip for the Study of Cholesterol–Protein Interactions Using SPR
Authors:
Peng He1,2,†, Shannon Faris1,2,†, Reddy Sudheer Sagabala3, Payel Datta1,2, Zihan Xu4, Brian Callahan4, Chunyu Wang1,2, Benoit Boivin3, Fuming Zhang2,5,* and Robert J. Linhardt1,2,5,*
Affiliation:
- Department of Chemistry and Chemical Biology, Rensselaer Polytechnic Institute, Troy, NY 12180, USA
- Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, NY 12180, USA
- Department of Nanobioscience, College of Nanoscale Science and Engineering, SUNY Polytechnic Institute, Albany, NY 12203, USA
- Department of Chemistry, Binghamton University, Binghamton, NY 13902, USA
- Departments of Chemical and Biological Engineering, Rensselaer Polytechnic Institute, Troy, NY 12180, USA
Description:
Cholesterol, an important lipid in animal membranes, binds to hydrophobic pockets within many soluble proteins, transport proteins and membrane bound proteins. The study of cholesterol–protein interactions in aqueous solutions is complicated by cholesterol’s low solubility and often requires organic co-solvents or surfactant additives. We report the synthesis of a biotinylated cholesterol and immobilization of this derivative on a streptavidin chip. Surface plasmon resonance (SPR) was then used to measure the kinetics of cholesterol interaction with cholesterol-binding proteins, hedgehog protein and tyrosine phosphatase 1B.
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