The effects of the oxidized phospholipids (oxPLs) on amyloid fibril formation by the apolipoprotein A-I variant 1-83/G26R have been investigated using Thioflavin T fluorescence assay. All types of the PoxnoPC assemblies (dispersions, micelles and lipid bilayer vesicles) induced retardation of amyloid nucleation and elongation and the enhancement of the 1-83/G26R fibrillization, although PazePC micelles completely prevented protein aggregation at low protein-to-lipid molar ratios. The ability of PazePC to inhibit 1-83/G26R aggregation was explained by the protein-lipid electrostatic interactions, which either stabilize the α-helical structure of the membrane-associated 1-83/G26R or facilitate the protein solubilization by the detergent micelles.
|Number of pages||6|
|Journal||Chemical Physics Letters|
|Publication status||Published - 16 Nov 2017|
|MoE publication type||A1 Journal article-refereed|