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The interaction of amyloid A beta(1-40) with lipid bilayers and ganglioside as studied by P-31 solid-state NMR

Nakazawa, Y., Suzuki, Y., Williamson, M.P., Saito, H. and Asakura, T. (2009) The interaction of amyloid A beta(1-40) with lipid bilayers and ganglioside as studied by P-31 solid-state NMR. Chemistry and Physics of Lipids, 158 (1). pp. 54-60. ISSN 0009-3084


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Amyloid P-peptide (A beta) is a major component of plaques in Alzheimer's disease, and formation of senile plaques has been suggested to originate fro m regions of neuronal membrane rich in gangliosides. We analyzed the mode of interaction of A beta with lipid bilayers by multinuclear NMR using P-31 nuclei. We found that A beta (1-40) strongly perturbed the bilayer structure of dimyristoylphosphatidylcholine (DMPQ, to form a non-lamellar phase (most likely micellar). The ganglioside GM1 potentiated the effect of A beta (1-40), as viewed from P-31 NMR. The difference of the isotropic peak intensity between DMPC/A beta and DMPC/GM1/A beta suggests a specific interaction between A beta and GM1. We show that in the DMPC/GM1/A beta system there are three lipid phases, namely a lamellar phase, a hexagonal phase and non-oriented lipids. The latter two phases are induced by the presence of the A beta peptide, and facilitated by GM1. 9) 2008 Elsevier Ireland Ltd. All rights reserved.

Item Type: Article
Copyright, Publisher and Additional Information: © 2008 Elsevier Ireland. This is an author produced version of a paper subsequently published in Chemistry and Physics of Lipids. Uploaded in accordance with the publisher's self-archiving policy.
Keywords: beta-Amyloid; Alzheimer's disease; NMR; GM1-ganglioside; Lipid bilayer
Institution: The University of Sheffield
Academic Units: The University of Sheffield > Faculty of Science (Sheffield) > School of Biological Sciences (Sheffield) > Department of Molecular Biology and Biotechnology (Sheffield)
Depositing User: Miss Anthea Tucker
Date Deposited: 28 Apr 2009 15:06
Last Modified: 08 Feb 2013 16:58
Published Version: http://dx.doi.org/10.1016/j.chemphyslip.2008.12.00...
Status: Published
Publisher: Elsevier Ireland
Refereed: Yes
Identification Number: 10.1016/j.chemphyslip.2008.12.001
URI: http://eprints.whiterose.ac.uk/id/eprint/8541

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