4.7 Article

Cholesterol Chip for the Study of Cholesterol-Protein Interactions Using SPR

Journal

BIOSENSORS-BASEL
Volume 12, Issue 10, Pages -

Publisher

MDPI
DOI: 10.3390/bios12100788

Keywords

cholesterol; cholesterol-binding proteins; surface plasmon resonance; binding kinetics; biotinylated cholesterol

Funding

  1. National Institutes of Health [S10OD028523, HL138605, R01 CA206592]
  2. National Science Foundation GlycoMIP [DMR 1933525]

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Cholesterol, an important lipid in animal cell membranes, can bind to various soluble proteins, transport proteins, and membrane-bound proteins. However, studying the interactions between cholesterol and proteins in aqueous solutions is challenging due to the low solubility of cholesterol, often necessitating the use of organic co-solvents or surfactant additives. In this study, a biotinylated cholesterol derivative was synthesized and immobilized on a streptavidin chip for analysis using surface plasmon resonance (SPR). The kinetics of cholesterol interactions with cholesterol-binding proteins, hedgehog protein and tyrosine phosphatase 1B, were determined.
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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