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Scanning tunnelling microscopy studies of beta-amyloid fibril structure and assembly.
Shivji, A P; Brown, F; Davies, M C; Jennings, K H; Roberts, C J; Wilkinson, M J; Williams, P M.
  • Shivji AP; Department of Pharmaceutical Sciences, University of Nottingham, UK.
FEBS Lett ; 371(1): 25-8, 1995 Aug 28.
Article en En | MEDLINE | ID: mdl-7664877
ABSTRACT
Alzheimer's disease is in part characterised by the deposit of beta-amyloid peptide in the form of fibrils in the brain. In this study, the scanning tunnelling microscope (STM) has been used to provide high resolution images of synthetic fibril structure and formation as a function of time. Short fibrils are observed following brief peptide incubation times. At longer incubation periods ribbon like filaments were observed. These results suggest that beta-amyloid self-assembly is an ordered process, with a correlation between time of incubation and length of beta-amyloid filament growth.
Asunto(s)
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Banco de datos: MEDLINE Asunto principal: Péptidos beta-Amiloides Idioma: En Año: 1995 Tipo del documento: Article
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Banco de datos: MEDLINE Asunto principal: Péptidos beta-Amiloides Idioma: En Año: 1995 Tipo del documento: Article