Journal article
Apolipoprotein C-II Adopts Distinct Structures in Complex with Micellar and Submicellar Forms of the Amyloid-Inhibiting Lipid-Mimetic Dodecylphosphocholine
TM Ryan, MDW Griffin, DJ McGillivray, RB Knott, K Wood, CL Masters, N Kirby, CC Curtain
Biophysical Journal | CELL PRESS | Published : 2016
Abstract
The formation of amyloid deposits is a common feature of a broad range of diseases, including atherosclerosis, Alzheimer's disease, and Parkinson's disease. The basis and role of amyloid deposition in the pathogenesis of these diseases is still being defined, however an interesting feature of amyloidogenic proteins is that the majority of the pathologically associated proteins are involved in lipid homeostasis, be it in lipid transport, incorporation into membranes, or the regulation of lipid pathways. Thus, amyloid-forming proteins commonly bind lipids, and lipids are generally involved in the proper folding of these proteins. However, understanding of the basis for these lipid-related aspe..
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Grants
Awarded by Australian Research Council
Funding Acknowledgements
This work was supported by the Australian National Health and Medical Research Council Program grant 628946. The Florey Institute is supported by Operational Infrastructure Support funding from the Victorian State Government. M.D.W.G. is the recipient of the C.R. Roper Fellowship and an Australian Research Council Future Fellowship (project No. FT140100544). This research was undertaken on the SAXS/WAXS beamline at the Australian Synchrotron, Victoria, Australia. We acknowledge valuable discussions with Dr. Cy Jeffries, which influenced the experimental design.