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Surface behaviour and lipid interaction of Alzheimer beta-amyloid peptide 1-42: a membrane-disrupting peptide

Ambroggio, Ernesto E., Kim, Dennis H., Separovic, Frances, Barrow, Colin J., Barnham, Kevin J., Bagatolli, Luis A. and Fidelio, Gerado D. 2005, Surface behaviour and lipid interaction of Alzheimer beta-amyloid peptide 1-42: a membrane-disrupting peptide, Biophysical journal, vol. 88, no. 4, pp. 2706-2713.

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Title Surface behaviour and lipid interaction of Alzheimer beta-amyloid peptide 1-42: a membrane-disrupting peptide
Author(s) Ambroggio, Ernesto E.
Kim, Dennis H.
Separovic, Frances
Barrow, Colin J.
Barnham, Kevin J.
Bagatolli, Luis A.
Fidelio, Gerado D.
Journal name Biophysical journal
Volume number 88
Issue number 4
Start page 2706
End page 2713
Total pages 8
Publisher Biophysical Society
Place of publication Bethesda, Md.
Publication date 2005
ISSN 0006-3495
1542-0086
Summary Amyloid aggregates, found in patients that suffer from Alzheimer's disease, are composed of fibril-forming peptides in a β-sheet conformation. One of the most abundant components in amyloid aggregates is the β-amyloid peptide 1–42 (Aβ 1–42). Membrane alterations may proceed to cell death by either an oxidative stress mechanism, caused by the peptide and synergized by transition metal ions, or through formation of ion channels by peptide interfacial self-aggregation. Here we demonstrate that Langmuir films of Aβ 1–42, either in pure form or mixed with lipids, develop stable monomolecular arrays with a high surface stability. By using micropipette aspiration technique and confocal microscopy we show that Aβ 1–42 induces a strong membrane destabilization in giant unilamellar vesicles composed of palmitoyloleoyl-phosphatidylcholine, sphingomyelin, and cholesterol, lowering the critical tension of vesicle rupture. Additionally, Aβ 1–42 triggers the induction of a sequential leakage of low- and high-molecular-weight markers trapped inside the giant unilamellar vesicles, but preserving the vesicle shape. Consequently, the Aβ 1–42 sequence confers particular molecular properties to the peptide that, in turn, influence supramolecular properties associated to membranes that may result in toxicity, including: 1), an ability of the peptide to strongly associate with the membrane; 2), a reduction of lateral membrane cohesive forces; and 3), a capacity to break the transbilayer gradient and puncture sealed vesicles.
Language eng
Field of Research 029901 Biological Physics
Socio Economic Objective 970102 Expanding Knowledge in the Physical Sciences
HERDC Research category C1.1 Refereed article in a scholarly journal
Copyright notice ©2005, Elsevier
Persistent URL http://hdl.handle.net/10536/DRO/DU:30023803

Document type: Journal Article
Collections: School of Life and Environmental Sciences
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Every reasonable effort has been made to ensure that permission has been obtained for items included in DRO. If you believe that your rights have been infringed by this repository, please contact drosupport@deakin.edu.au.