title: [Electron microscopic study of the influence of fullerene on the formation of amyloid fibrils by A beta(25-35) peptide].
abstract: The anti-amyloidogenic capacity of hydrated fullerene C60 HyFn was revealed by the use of electron microscopy. We first showed that when, connecting with growing amyloid fibrils formed by A beta(25-35)-peptide, fullerene prevented their subsequent growth and interfered with the formation of new fibrils. Instead of long helically twisted ribbons formed by A beta(25-35)-peptide in the absence of fullerene, short narrow protofibrils were found in the presence of fullerene . These results allow one to suppose that fullerene can be useful for the therapy of Alzheimer's disease.
authors.forename: Z A
authors.initials: ZA
authors.lastname: Podlubnaia
authors.forename: I Ia
authors.initials: IIa
authors.lastname: Podol'skiĭ
authors.forename: M D
authors.initials: MD
authors.lastname: Shpagina
authors.forename: L G
authors.initials: LG
authors.lastname: Marsagishvili
mesh_terms: D000682:Amyloid / Q000737:chemistry*; D016229:Amyloid beta-Peptides / Q000737:chemistry*; D037741:Fullerenes / Q000737:chemistry*; D008854:Microscopy, Electron; D010446:Peptide Fragments / Q000737:chemistry*
chemical_list: D000682:Amyloid; D016229:Amyloid beta-Peptides; D037741:Fullerenes; D010446:Peptide Fragments; C074636:amyloid beta-protein (25-35)