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Nanoscale Imaging and Characterisation of Amyloid-β

  • Book
  • © 2016

Overview

Authors:
  1. Claire Louisa Tinker-Mill

    1. Research and Enterprise Services, Lancaster University , Lancaster, United Kingdom

    View author publications

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  • Nominated as an outstanding Ph.D. thesis by the Lancaster University, UK
  • Presents a detailed study of amyloid-beta using multiple methods of atomic force microscopy
  • Author received the 2012 and 2014 Juno Award for Research Excellence from Lancaster University
  • Includes supplementary material: sn.pub/extras

Part of the book series: Springer Theses (Springer Theses)

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Table of contents (9 chapters)

  1. Front Matter

    Pages i-xx
    Download chapter PDF

  2. Introduction

    • Claire Louisa Tinker-Mill
    Pages 1-5

  3. Theoretical Concepts of Scanning Probe Microscopy and Dynamic Light Scattering and Their Relation to the Study of Peptide Nanostructures

    • Claire Louisa Tinker-Mill
    Pages 7-30

  4. Alzheimer’s Disease and the Aggregation of Amyloid β

    • Claire Louisa Tinker-Mill
    Pages 31-52

  5. Experimental Methodology

    • Claire Louisa Tinker-Mill
    Pages 53-72

  6. Substrate Development of the Imaging of Amyloid Proteins with SPM Methods

    • Claire Louisa Tinker-Mill
    Pages 73-86

  7. Scanning Probe Microscopy Methods of Imaging Amyloid Peptides During the Aggregation Process

    • Claire Louisa Tinker-Mill
    Pages 87-106

  8. Spectroscopy and Thermal SPM Methods of Studying Aβ1:42

    • Claire Louisa Tinker-Mill
    Pages 107-119

  9. The Application of Biophysical Techniques to the Study of the Inhibition of Aggregation of Aβ Using PINPs Liposomes

    • Claire Louisa Tinker-Mill
    Pages 121-137

  10. Conclusion and Future Perspectives

    • Claire Louisa Tinker-Mill
    Pages 139-149
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Keywords

About this book

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.


Authors and Affiliations

  • Research and Enterprise Services, Lancaster University , Lancaster, United Kingdom

    Claire Louisa Tinker-Mill

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