Membrane disordering effects of beta-amyloid peptides.
The interaction of Abeta with synaptosomal plasma membranes decreases membrane fluidity. Using model membrane/liposome systems the interaction of Abeta with specific lipids (e.g. phospholipids, gangliosides, cholesterol) has been defined. The formation of the beta-sheet structure of Abeta when undergoing peptide aggregation is important for Abeta's membrane perturbing properties. This effect can be correlated with the peptide length of Abeta, the longer Abeta1-42 having the greatest effect on membrane fluidity and on neurotoxicity.
Eckert
Gunter P
GP
Department of Pharmacology, ZAFES, Biocenter University of Frankfurt, Germany.
Wood
W G
WG
Müller
W E
WE
D000544:Alzheimer Disease / Q000378:metabolism / Q000473:pathology; D016229:Amyloid beta-Peptides / Q000737:chemistry / Q000378:metabolism*; D000818:Animals; D002462:Cell Membrane / Q000648:ultrastructure*; D002784:Cholesterol / Q000378:metabolism; D006801:Humans; D007425:Intracellular Membranes / Q000648:ultrastructure*; D008560:Membrane Fluidity; D008563:Membrane Lipids / Q000378:metabolism; D051379:Mice; D011487:Protein Conformation; D051381:Rats; D013574:Synaptosomes / Q000378:metabolism
D016229:Amyloid beta-Peptides; D008563:Membrane Lipids; D002784:Cholesterol