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

Research output: Contribution to journalArticle

Researchers

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

Research units

  • V. N. Karazin Kharkiv National University
  • University of Helsinki
  • Kyoto Pharmaceutical University

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.

Details

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

ID: 15720146