Skip to main content
  • Book
  • © 2016

Nanoscale Imaging and Characterisation of Amyloid-β

  • 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)

Buy it now

Buying options

eBook USD 84.99
Price excludes VAT (USA)
  • Available as EPUB and PDF
  • Read on any device
  • Instant download
  • Own it forever
Softcover Book USD 109.99
Price excludes VAT (USA)
  • Compact, lightweight edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info
Hardcover Book USD 109.99
Price excludes VAT (USA)
  • Durable hardcover edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Other ways to access

This is a preview of subscription content, access via your institution.

Table of contents (9 chapters)

  1. Front Matter

    Pages i-xx
  2. Introduction

    • Claire Louisa Tinker-Mill
    Pages 1-5
  3. Alzheimer’s Disease and the Aggregation of Amyloid β

    • Claire Louisa Tinker-Mill
    Pages 31-52
  4. Experimental Methodology

    • Claire Louisa Tinker-Mill
    Pages 53-72
  5. Spectroscopy and Thermal SPM Methods of Studying Aβ1:42

    • Claire Louisa Tinker-Mill
    Pages 107-119
  6. Conclusion and Future Perspectives

    • Claire Louisa Tinker-Mill
    Pages 139-149

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.


Keywords

  • AFM Imaging of Amyloid-beta
  • Nanomechanical Characterisation
  • Alzheimer's Disease and AFM
  • Aggregation of Amyloid-beta
  • Ultrasonic Force Microscopy

Authors and Affiliations

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

    Claire Louisa Tinker-Mill

Bibliographic Information

Buy it now

Buying options

eBook USD 84.99
Price excludes VAT (USA)
  • Available as EPUB and PDF
  • Read on any device
  • Instant download
  • Own it forever
Softcover Book USD 109.99
Price excludes VAT (USA)
  • Compact, lightweight edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info
Hardcover Book USD 109.99
Price excludes VAT (USA)
  • Durable hardcover edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Other ways to access