Scanning tunnelling microscopy studies of beta-amyloid fibril structure and assembly.
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.
Shivji
A P
AP
Department of Pharmaceutical Sciences, University of Nottingham, UK.
Brown
F
F
Davies
M C
MC
Jennings
K H
KH
Roberts
C J
CJ
Tendler SJf
Wilkinson
M J
MJ
Williams
P M
PM
D000595:Amino Acid Sequence; D016229:Amyloid beta-Peptides / Q000096:biosynthesis* / Q000138:chemical synthesis / Q000737:chemistry / Q000648:ultrastructure*; D016252:Microscopy, Scanning Tunneling; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000138:chemical synthesis
D016229:Amyloid beta-Peptides; D010446:Peptide Fragments