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Nanoscale Imaging and Characterisation of Amyloid-β - Claire Louisa Tinker-Mill (Springer, 2016) pdf

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 							ISBN 978-3-319-39533-3
  
  This thesis presents a method for reliably and robustly producing samples
of amyloid-β (Aβ) by capturing them at various stages of aggregation, as well as the results of subsequent imaging
with various atomic force microscopy (AFM) methods, all of which add value to the data gathered by collecting
information on the peptide’s nanomechanical, elastic, thermal or spectroscopical properties. 
  Amyloid-β
(Aβ) undergoes a hierarchy of aggregation following a structural transition, making it an ideal subject of study
using scanning probe microscopy (SPM), dynamic light scattering (DLS) and other physical techniques. By imaging samples
of Aβ with Ultrasonic Force Microscopy, a detailed substructure to the morphology is revealed, which correlates well
with the most advanced cryo-EM work. Early stage work in the area of thermal and spectroscopical AFM is also presented,
and indicates the promise these techniques may hold for imaging sensitive and complex biological materials. This thesis
demonstrates that physical techniques can be highly complementary when studying the aggregation of amyloid peptides, and
allow the detection of subtle differences in their aggregation processes. 						

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