Membrane domain modulation of Aβ1–42 oligomer interactions with supported lipid bilayers: an atomic force microscopy investigation-Reference-Cited by-同舟云学术

Membrane domain modulation of Aβ1–42 oligomer interactions with supported lipid bilayers: an atomic force microscopy investigation

Published:2019 Issue:43 Volume:11 Page:20857-20867
ISSN:2040-3364
Container-title:Nanoscale
language:en
Short-container-title:Nanoscale

Author:

Azouz Mehdi¹²³⁴⁵,Cullin Christophe¹²³⁴⁵^ORCID,Lecomte Sophie¹²³⁴⁵^ORCID,Lafleur Michel⁶⁷⁸⁹^ORCID

Affiliation:

1. Chimie et Biologie des Membranes et Nanoobjets

2. CBMN CNRS UMR 5248

3. Université de Bordeaux

4. Allée Geoffroy de Saint-Hilaire

5. 33600 Pessac

6. Department of Chemistry

7. Université de Montréal

8. Montréal

9. Canada

Abstract

Lipid domains favour membrane perturbations induced by Aβ_1–42, an amyloid peptide identified as a trigger of Alzheimer's disease. It is proposed that lipid packing defects at domain interfaces could act as adsorption and nucleation sites.

Funder

Natural Sciences and Engineering Research Council of Canada

Fonds Québécois de la Recherche sur la Nature et les Technologies

Publisher

Royal Society of Chemistry (RSC)

Subject

General Materials Science

Link

http://pubs.rsc.org/en/content/articlepdf/2019/NR/C9NR06361G

Reference80 articles.

1. Alzheimer's Disease: Genes, Proteins, and Therapy

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4. A Structure-Toxicity Study of Aß42 Reveals a New Anti-Parallel Aggregation Pathway

5. Interaction of Aβ1–42 Amyloids with Lipids Promotes “Off-Pathway” Oligomerization and Membrane Damage

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