Journal article
Europium as an inhibitor of Amyloid-β(1-42) induced membrane permeation
FEBS letters, v 589(21), pp 3228-3236
24 Oct 2015
PMID: 26450778
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
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•Europium ions complex with GM1 gangliosides in phospholipid membranes.•Europium ions cause inhibition Aβ–membrane interactions.•Europium blocks an Aβ receptor protecting against membrane permeation.•Discrete Aβ binding events correlate to specific membrane permeation events.
Soluble Amyloid-beta (Aβ) oligomers are a source of cytotoxicity in Alzheimer’s disease (AD). The toxicity of Aβ oligomers may arise from their ability to interact with and disrupt cellular membranes mediated by GM1 ganglioside receptors within these membranes. Therefore, inhibition of Aβ–membrane interactions could provide a means of preventing the toxicity associated with Aβ. Here, using Surface Plasmon field-enhanced Fluorescence Spectroscopy, we determine that the lanthanide, Europium III chloride (Eu3+), strongly binds to GM1 ganglioside-containing membranes and prevents the interaction with Aβ42 leading to a loss of the peptides ability to cause membrane permeation. Here we discuss the molecular mechanism by which Eu3+ inhibits Aβ42-membrane interactions and this may lead to protection of membrane integrity against Aβ42 induced toxicity.
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Details
- Title
- Europium as an inhibitor of Amyloid-β(1-42) induced membrane permeation
- Creators
- Thomas L Williams - School of Life Sciences, University of Sussex, Falmer, East Sussex BN1 9QG, UKBrigita Urbanc - Physics Department, Drexel University, Philadelphia, PA 19104, USAKaren E Marshall - School of Life Sciences, University of Sussex, Falmer, East Sussex BN1 9QG, UKDevkee M Vadukul - School of Life Sciences, University of Sussex, Falmer, East Sussex BN1 9QG, UKA. Toby A Jenkins - Department of Chemistry, University of Bath, Bath BA2 7AY, UKLouise C Serpell - School of Life Sciences, University of Sussex, Falmer, East Sussex BN1 9QG, UK
- Publication Details
- FEBS letters, v 589(21), pp 3228-3236
- Publisher
- Elsevier
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Physics
- Web of Science ID
- WOS:000364604900002
- Scopus ID
- 2-s2.0-84944930612
- Other Identifier
- 991014877772304721
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- Collaboration types
- Domestic collaboration
- International collaboration
- Web of Science research areas
- Biochemistry & Molecular Biology
- Biophysics
- Cell Biology