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Papers In Press, published online ahead of print February 17, 2007
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Gladstone Institute of Neurological Disease, UCSF, The J. David Gladstone Institutes, San Francisco, CA 94158
Corresponding Author: kweisgraber{at}gladstone.ucsf.edu
Apolipoprotein (apo) E is a major protein component of cholesterol-transporting lipoprotein particles in the central nervous system and in plasma. Polymorphisms of apoE are associated with cardiovascular disease and with a predisposition to Alzheimer’s disease and other forms of neurodegeneration. For full biological activity, apoE must be bound to a lipoprotein particle. Complexes of apoE and phospholipid mimic many of these activities. In contrast to a widely accepted discoidal model of apo A-I bound to dimyristoylphosphatidylcholine, which is based on solution studies, an x-ray diffraction study of apoE bound to dipalmitoylphosphatidylcholine (DPPC) indicated that apoE•DPPC particles are quasi-spheroidal and that the packing of the phospholipid core is similar to a micelle. Using small-angle x-ray scattering, we show that apoE•DPPC particles in solution are ellipsoidal and that the shape of the phospholipid core is compatible with a twisted bilayer model. The proposed model is consistent with the results of mass spectrometric analysis of products of limited proteolysis. These revealed that the non-lipid bound regions of apoE in the particle are consistent with an a-helical hairpin.
Revised on February 15, 2007
Accepted on February 16, 2007
Apolipoprotein E.dipalmitoylphosphatidylcholine particles are ellipsoidal in solution
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