Abstract
Apolipoproteins are proteins which bind to lipids, forming lipoprotein complexes to encapsulate cholesterol and triglycerides. Structure and transport of lipoproteins are regulated by the binding of specific apolipoproteins where they serve as receptors and ligands. Apolipoprotein C-III (apoCIII) inhibits hydrolysis of lipids by lipase. Elevated levels of apoCIII are associated with hypertriglyceridemia and an increased risk of coronary heart disease. Despite its importance in lipid metabolism, fundamental lipid binding properties of apoCIII remain to be characterized. Using unilamellar vesicles with varied lipid composition and curvature, we apply fluorescence correlation spectroscopy, circular dichroism spectroscopy, and transmission electron microscopy to determine membrane binding affinity, secondary structure formation, and membrane integrity, respectively.
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