title: Misfolding of amyloidogenic proteins at membrane surfaces: the impact of macromolecular crowding.
abstract: The presence of inert macromolecular crowding agents mimics the situation in vivo where amyloidogenic proteins are released into an aqueous, congested intracellular environment. By using the amphiphatic Alzheimer Abeta-protein as the model system, the presence of a three-dimensional macromolecular crowding environment enhanced significantly its misfolding behavior if charged membrane surfaces as two-dimensional aggregation templates were present.
authors.affiliation: Department of Chemistry, University of Umeå, 90187 Umeå, Sweden.
authors.forename: Marcus
authors.initials: M
authors.lastname: Bokvist
authors.forename: Gerhard
authors.initials: G
authors.lastname: Gröbner
mesh_terms: D000682:Amyloid / Q000737:chemistry* / Q000378:metabolism*; D002942:Circular Dichroism; D008567:Membranes, Artificial; D017510:Protein Folding; D017433:Protein Structure, Secondary
chemical_list: D000682:Amyloid; D008567:Membranes, Artificial