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Scanning tunnelling microscopy studies of β‐amyloid fibril structure and assembly
Author(s) -
Shivji A.P.,
Brown F.,
Davies M.C.,
Jennings K.H.,
Roberts C.J.,
Tendler S.J.B.,
Wilkinson M.J.,
Williams P.M.
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)00858-7
Subject(s) - fibril , protein filament , biophysics , amyloid (mycology) , peptide , amyloid fibril , chemistry , incubation , microscopy , crystallography , amyloid β , biology , biochemistry , optics , pathology , physics , disease , medicine , inorganic chemistry
Alzheimer's disease is in part characterised by the deposit of β‐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 β‐amyloid self‐assembly is an ordered process, with a correlation between time of incubation and length of β‐amyloid filament growth.