Fluorescence study of the effect of the oxidized phospholipids on amyloid fibril formation by the apolipoprotein A-I N-terminal fragment

Kateryna Vus*, Mykhailo Girych, Valeriya Trusova, Galyna Gorbenko, Paavo Kinnunen, Chiharu Mizuguchi, Hiroyuki Saito

*Corresponding author for this work

Research output: Contribution to journalArticleScientificpeer-review

3 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)1-6
Number of pages6
JournalChemical Physics Letters
Volume688
DOIs
Publication statusPublished - 16 Nov 2017
MoE publication typeA1 Journal article-refereed

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