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Sub‐micellar phospholipid accelerates amyloid formation by apolipoprotein C‐II
Author(s) -
Hatters Danny M.,
Lawrence Lynne J.,
Howlett Geoffrey J.
Publication year - 2001
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(01)02355-9
Subject(s) - phospholipid , chemistry , amyloid (mycology) , apolipoprotein b , biophysics , micelle , folding (dsp implementation) , amyloid fibril , biochemistry , cholesterol , amyloid β , membrane , biology , aqueous solution , organic chemistry , medicine , inorganic chemistry , disease , electrical engineering , engineering
Lipid‐free human apolipoprotein C‐II (apoC‐II) forms amyloid fibrils with characteristic β‐structure. This conformation is distinct from the α‐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 α‐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.