In-situ atomic force microscopy study of β-amyloid fibrillization

We report the use of atomic force microscopy to observe the initial stages of β-amyloid fibrillization in situ. The growth of individual β-amyloid protofibrils on a mica substrate was followed over several hours. The first in situ visualization of protofibril formation from single aggregate units of...

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Bibliographic Details
Published in:	Journal of molecular biology Vol. 298; no. 5; pp. 833 - 840
Main Authors:	Blackley, H.K.L, Sanders, G.H.W, Davies, M.C, Roberts, C.J, Tendler, S.J.B, Wilkinson, M.J
Format:	Journal Article
Language:	English
Published:	England Elsevier Ltd 19-05-2000
Subjects:	Adsorption Aluminum Silicates Alzheimer’s disease Amyloid beta-Peptides - chemistry Amyloid beta-Peptides - metabolism Amyloid beta-Peptides - ultrastructure atomic force microscopy Biopolymers - chemistry Biopolymers - metabolism fibril formation Kinetics Microscopy, Atomic Force Models, Biological Monte Carlo Method Peptide Fragments - chemistry Peptide Fragments - metabolism Peptide Fragments - ultrastructure Protein Binding Protein Structure, Quaternary protofibril Solutions Time Factors β-amyloid protofibril AFM fibril formation Alzheimer’s disease atomic force microscopy β-amyloid
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Summary:	We report the use of atomic force microscopy to observe the initial stages of β-amyloid fibrillization in situ. The growth of individual β-amyloid protofibrils on a mica substrate was followed over several hours. The first in situ visualization of protofibril formation from single aggregate units of β-amyloid is reported. The growth of these protofibrils through the subsequent addition of these aggregate units is also observed. Growth of the protofibrils is bi-directional and the outgrowth of protofibrils from a common amyloid/heterogeneous core is also observed. Elongation also occurred by the addition of protofibrils from solution. This data provides an exciting insight into the early stages of β-amyloid fibrillization and can be used to enhance the understanding of the mechanism(s) by which β-amyloid fibrillizes and may consequently enable inhibition of one or more stages of fibrillization as a potential therapeutic strategy.
Bibliography:	ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 23 ObjectType-Article-1 ObjectType-Feature-2
ISSN:	0022-2836 1089-8638
DOI:	10.1006/jmbi.2000.3711