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Dependence of Apolipoprotein C-III membrane binding properties on lipid composition and membrane curvature.

Wednesday, November 06, 2013 — Poster Session I

4:00 p.m. – 6:00 p.m.

FAES Academic Center (Upper-Level Terrace)




  • M. de Messieres
  • Y. He
  • J. C. Lee


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-3 (ApoC3) inhibits hydrolysis of lipids by lipase. Elevated levels of ApoC3 are associated with hypertriglyceridemia and an increased risk of coronary heart disease. Despite its importance in lipid metabolism, fundamental lipid binding properties of ApoC3 remain to be characterized. Using unilamellar vesicles with varied lipid composition and curvature, we apply single-liposome microscopy, circular dichroism spectroscopy, and transmission electron microscopy to determine membrane binding affinity, secondary structure formation, and membrane integrity, respectively.

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