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

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Vus , K , Girych , M , Trusova , V , Gorbenko , G , Kinnunen , P , Mizuguchi , C & Saito , H 2017 , ' Fluorescence study of the effect of the oxidized phospholipids on amyloid fibril formation by the apolipoprotein A-I N-terminal fragment ' , Chemical Physics Letters , vol. 688 , pp. 1-6 . https://doi.org/10.1016/j.cplett.2017.09.037

Title: Fluorescence study of the effect of the oxidized phospholipids on amyloid fibril formation by the apolipoprotein A-I N-terminal fragment
Author: Vus, Kateryna; Girych, Mykhailo; Trusova, Valeriya; Gorbenko, Galyna; Kinnunen, Paavo; Mizuguchi, Chiharu; Saito, Hiroyuki
Contributor: University of Helsinki, Department of Physics
Date: 2017-11-16
Language: eng
Number of pages: 6
Belongs to series: Chemical Physics Letters
ISSN: 0009-2614
URI: http://hdl.handle.net/10138/307419
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 a-helical structure of the membrane-associated 1-83/G26R or facilitate the protein solubilization by the detergent micelles. (C) 2017 Elsevier B.V. All rights reserved.
Subject: HIGH-DENSITY-LIPOPROTEINS
ACYL-CHAIN REVERSAL
PROTEIN AGGREGATION
MEMBRANE-PROTEINS
OXIDATIVE STRESS
THIOFLAVINE-T
PHOSPHATIDYLCHOLINES
DISEASES
ALZHEIMERS
BIOPHYSICS
116 Chemical sciences
114 Physical sciences
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