Differences between amyloid-β aggregation in solution and on the membrane: insights into elucidation of the mechanistic details of Alzheimer's disease.
The association of the amyloid-β (Aβ) peptide with cellular membranes is hypothesized to be the underlying phenomenon of neurotoxicity in Alzheimer's disease. Misfolding of proteins and peptides, as is the case with Aβ, follows a progression from a monomeric state, through intermediates, ending at long, unbranched amyloid fibers. This tutorial review offers a perspective on the association of toxic Aβ structures with membranes as well as details of membrane-associated mechanisms of toxicity.
Biophysics and Department of Chemistry, University of Michigan, 930 N. University Ave, Ann Arbor, MI 48109-1055, USA. ramamoor@umich.edu.
Samuel A
SA
Kotler
Patrick
P
Walsh
Jeffrey R
JR
Brender
Ayyalusamy
A
Ramamoorthy
D000544:Alzheimer Disease / Q000378:metabolism / Q000473:pathology*; D016229:Amyloid beta-Peptides / Q000737:chemistry / Q000378:metabolism*; D002462:Cell Membrane / Q000737:chemistry / Q000378:metabolism*; D005732:Gangliosides / Q000737:chemistry / Q000378:metabolism; D006801:Humans; D017433:Protein Structure, Secondary; D012996:Solutions / Q000737:chemistry
D016229:Amyloid beta-Peptides; D005732:Gangliosides; D012996:Solutions