The two-fold aspect of the interplay of amyloidogenic proteins with lipid membranes.
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 amyloid 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 amyloid-membrane interactions is emphasized.
Relini
Annalisa
A
Department of Physics, University of Genoa, Via Dodecaneso 33, 16146 Genoa, Italy.
Cavalleri
Ornella
O
Rolandi
Ranieri
R
Gliozzi
Alessandra
A
D000682:Amyloid / Q000378:metabolism*; D000818:Animals; D002462:Cell Membrane / Q000378:metabolism*; D002463:Cell Membrane Permeability / Q000502:physiology*; D006801:Humans; D008051:Lipid Bilayers / Q000378:metabolism*; D018625:Microscopy, Atomic Force; D011485:Protein Binding / Q000502:physiology; D011487:Protein Conformation
D000682:Amyloid; D008051:Lipid Bilayers