Header

UZH-Logo

Maintenance Infos

Amyloid-β Peptide–Lipid Bilayer Interaction Investigated by Supercritical Angle Fluorescence


Dubois, Valentin; Serrano, Diana; Seeger, Stefan (2019). Amyloid-β Peptide–Lipid Bilayer Interaction Investigated by Supercritical Angle Fluorescence. ACS Chemical Neuroscience, 10(12):4776-4786.

Abstract

The understanding of the interaction between the membrane of neurons and amyloid-beta peptides is of crucial importance to shed light on the mechanism of toxicity in Alzheimer's disease. This paper describes how supercritical angle fluorescence spectroscopy was applied to monitor in real-time the interaction between a supported lipid bilayer (SLB) and the peptide. Different forms of amyloid-beta (40 and 42 amino acids composition) were tested, and the interfacial fluorescence was measured to get information about the lipid integrity and mobility. The results show a concentration-dependent damaging process of the lipid bilayer. Prolonged interaction with the peptide up to 48 h lead to an extraction and clustering of lipid molecules from the surface and a potential disruption of the bilayer, correlated with the formation of peptide aggregates. The natural diffusion of the lipid was slightly hindered by the interaction with amyloid-beta(1-42) and closely related to the oligomerization of the peptide. The adsorption and desorption of Amyloid-beta was also characterized in terms of affinity. Amyloid-beta(1-42) exhibited a slightly higher affinity than amyloid-beta(1-40). The former was also more prone to aggregate and to adsorb on the bilayer as oligomer.

Abstract

The understanding of the interaction between the membrane of neurons and amyloid-beta peptides is of crucial importance to shed light on the mechanism of toxicity in Alzheimer's disease. This paper describes how supercritical angle fluorescence spectroscopy was applied to monitor in real-time the interaction between a supported lipid bilayer (SLB) and the peptide. Different forms of amyloid-beta (40 and 42 amino acids composition) were tested, and the interfacial fluorescence was measured to get information about the lipid integrity and mobility. The results show a concentration-dependent damaging process of the lipid bilayer. Prolonged interaction with the peptide up to 48 h lead to an extraction and clustering of lipid molecules from the surface and a potential disruption of the bilayer, correlated with the formation of peptide aggregates. The natural diffusion of the lipid was slightly hindered by the interaction with amyloid-beta(1-42) and closely related to the oligomerization of the peptide. The adsorption and desorption of Amyloid-beta was also characterized in terms of affinity. Amyloid-beta(1-42) exhibited a slightly higher affinity than amyloid-beta(1-40). The former was also more prone to aggregate and to adsorb on the bilayer as oligomer.

Statistics

Citations

Altmetrics

Downloads

0 downloads since deposited on 07 Feb 2020
0 downloads since 12 months

Additional indexing

Item Type:Journal Article, refereed, original work
Communities & Collections:07 Faculty of Science > Department of Chemistry
Dewey Decimal Classification:540 Chemistry
Uncontrolled Keywords:Cell Biology, Biochemistry, Physiology, Cognitive Neuroscience, General Medicine
Language:English
Date:18 December 2019
Deposited On:07 Feb 2020 13:58
Last Modified:07 Feb 2020 13:58
Publisher:American Chemical Society (ACS)
ISSN:1948-7193
Additional Information:This document is the Accepted Manuscript version of a Published Work that appeared in final form in Chemical Neuroscience, © American Chemical Society after peer review and technical editing by the publisher. To access the final edited and published work see 10.1021/acschemneuro.9b00264
OA Status:Closed
Free access at:Publisher DOI. An embargo period may apply.
Publisher DOI:https://doi.org/10.1021/acschemneuro.9b00264
Project Information:
  • : FunderSwiss National Science Foundation (SNSF)
  • : Grant ID
  • : Project Title

Download

Closed Access: Download allowed only for UZH members

Content: Accepted Version
Filetype: PDF - Registered users only until 25 May 2020
Size: 1MB
View at publisher
Embargo till: 2020-05-25