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Assembly of lipids and proteins into lipoprotein particles

Journal of Physical Chemistry B, ISSN: 1520-6106, Vol: 111, Issue: 38, Page: 11095-11104
2007
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Article Description

The self-assembly of reconstituted discoidal high-density lipoproteins, known as nanodiscs, was studied using coarse-grained molecular dynamics and small-angle X-ray scattering. In humans, high-density lipoprotein particles transport cholesterol in the blood and facilitate the removal of excess cholesterol from the body. Native high-density lipoprotein exhibits a wide variety of shapes and sizes, forming lipid-free/poor, nascent discoidal, and mature spherical particles. Little is known about how these lipoprotein particles assemble and transform from one state to another. Multiple 10 μs coarse-grained simulations reveal the assembly of discoidal high-density lipoprotein particles from disordered protein-lipid complexes. Small-angle X-ray scattering patterns were calculated from the final assembled structures and compared with experimental measurements carried out for this study to verify the accuracy of the coarse-grained simulations. Results show that hydrophobic interactions assemble, within several microseconds, the amphipathic helical proteins and lipids into roughly discoidal particles, while the proteins assume a final approximate double-belt configuration on a slower time scale. © 2007 American Chemical Society.

Bibliographic Details

Shih, Amy Y; Arkhipov, Anton; Freddolino, Peter L; Sligar, Stephen G; Schulten, Klaus

American Chemical Society (ACS)

Chemistry; Materials Science

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