title: Copper-mediated growth of amyloid β fibrils in the presence of oxidized and negatively charged liposomes.
abstract: Amyloid β protein (Aβ) from Alzheimer's disease formed fibrillar aggregates and their morphology depended on oxidized and negatively charged liposomes. The morphology of fibrillar aggregates was affected by Cu(2+), together with their growth kinetics. This is because Cu(2+) inhibited the nucleation step in the formation of amyloid Aβ fibrillar aggregates by forming Aβ/Cu complex inactive to the growth of fibrillar aggregates. In addition, this is probably because Cu(2+) affected the fibrillar aggregate formed on the surface of liposomes. These findings would give a better understanding of the formation mechanism of amyloid fibrils on biomembranes.
authors.affiliation: Division of Chemical Engineering, Graduate School of Engineering Science, Osaka University, 1–3 Machikaneyama-cho, Toyonaka, Osaka 560–8531, Japan.
authors.forename: Toshinori
authors.initials: T
authors.lastname: Shimanouchi
authors.forename: Ryo
authors.initials: R
authors.lastname: Onishi
authors.forename: Nachi
authors.initials: N
authors.lastname: Kitaura
authors.forename: Hiroshi
authors.initials: H
authors.lastname: Umakoshi
authors.forename: Ryoichi
authors.initials: R
authors.lastname: Kuboi
mesh_terms: D000544:Alzheimer Disease / Q000378:metabolism; D000682:Amyloid / Q000037:antagonists & inhibitors / Q000378:metabolism*; D016229:Amyloid beta-Peptides / Q000378:metabolism*; D003300:Copper / Q000494:pharmacology*; D006801:Humans; D007425:Intracellular Membranes / Q000378:metabolism; D007700:Kinetics; D008081:Liposomes; D010084:Oxidation-Reduction
chemical_list: D000682:Amyloid; D016229:Amyloid beta-Peptides; D008081:Liposomes; D003300:Copper