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The two-fold aspect of the interplay of amyloidogenic proteins with lipid membranes

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CHEMISTRY AND PHYSICS OF LIPIDS
卷 158, 期 1, 页码 1-9

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ELSEVIER IRELAND LTD
DOI: 10.1016/j.chemphyslip.2008.11.003

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Amyloid aggregates; Phospholipid monolayers; Supported phospholipid bilayers; Membrane-assisted fibrillogenesis; AFM

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Investigating the pathways leading to the formation of amyloid protein aggregates and the mechanism of their cytotoxicity is fundamental for a deeper understanding of a broad range of human diseases. Increasing evidence indicates that early aggregates are responsible for the cytotoxic effects. This paper addresses the catalytic role of lipid surfaces in promoting aggregation of annyloid proteins and the permeability changes that these aggregates induce on lipid membranes. Effects of amyloid aggregates on model systems such as monolayers, vesicles, liposomes and supported lipid bilayers are reviewed. In particular, the relevance of atomic force microscopy in detecting both kinetics of amyloid formation and a mylold-membrane interactions is emphasized. (c) 2008 Elsevier Ireland Ltd. All rights reserved.

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