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Europium as an inhibitor of Amyloid-β(1-42) induced membrane permeation
- Williams, Thomas L., Urbanc, Brigita, Marshall, Karen E., Vadukul, Devkee M., Jenkins, A. Toby A., Serpell, Louise C.
- FEBS letters 2015 v.589 no.21 pp. 3228-3236
- Alzheimer disease, cell membranes, cytotoxicity, europium, fluorescence emission spectroscopy, gangliosides, peptides, receptors
- 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.