Amyloidogenic protein-membrane interactions: mechanistic insight from model systems.
The toxicity of amyloid-forming proteins is correlated with their interactions with cell membranes. Binding events between amyloidogenic proteins and membranes result in mutually disruptive structural perturbations, which are associated with toxicity. Membrane surfaces promote the conversion of amyloid-forming proteins into toxic aggregates, and amyloidogenic proteins, in turn, compromise the structural integrity of the cell membrane. Recent studies with artificial model membranes have highlighted the striking resemblance of the mechanisms of membrane permeabilization of amyloid-forming proteins to those of pore-forming toxins and antimicrobial peptides.
Butterfield
Sara M
SM
Laboratory of Molecular Neurobiology and Neuroproteomics, Swiss Federal Institute of Technology Lausanne (EPFL), SV-BMI-LMNN AI2351, 1015 Lausanne, Switzerland.
Lashuel
Hilal A
HA
D000682:Amyloid / Q000737:chemistry / Q000378:metabolism*; D016229:Amyloid beta-Peptides / Q000737:chemistry / Q000378:metabolism*; D002462:Cell Membrane / Q000378:metabolism*; D058228:Islet Amyloid Polypeptide / Q000737:chemistry / Q000378:metabolism*; D008055:Lipids / Q000737:chemistry; D008670:Metals / Q000737:chemistry; D008954:Models, Biological; D017510:Protein Folding; D013499:Surface Properties; D051843:Synucleins / Q000737:chemistry / Q000378:metabolism*
D000682:Amyloid; D016229:Amyloid beta-Peptides; D058228:Islet Amyloid Polypeptide; D008055:Lipids; D008670:Metals; D051843:Synucleins