Sub-micellar phospholipid accelerates amyloid formation by apolipoprotein C-II |
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Authors: | Hatters D M Lawrence L J Howlett G J |
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Institution: | Department of Biochemistry and Molecular Biology, The University of Melbourne, Parkville, Vic. 3010, Australia. |
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Abstract: | Lipid-free human apolipoprotein C-II (apoC-II) forms amyloid fibrils with characteristic beta-structure. This conformation is distinct from the alpha-helical fold of lipid-bound apoC-II. We have investigated the effect of the short-chain phospholipid, dihexanoylphosphatidylcholine (DHPC) on amyloid formation by apoC-II. The alpha-helical content of apoC-II increases in the presence of micellar DHPC (16 mM) and amyloid formation is inhibited. However, at sub-micellar DHPC concentrations (below 8 mM) amyloid formation is accelerated 6 fold. These results suggest that individual phospholipid molecules in vivo may exert significant effects on amyloid folding pathways. |
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