Amyloid Under the Atomic Force Microscope

Walraj S. Gosal; Sarah L. Myers; Sheena E. Radford; Neil H. Thomson

doi:10.2174/092986606775338498

ISSN: 0929-8665
E-ISSN: 1875-5305

Amyloid Under the Atomic Force Microscope
Authors: Walraj S. Gosal¹, Sarah L. Myers², Sheena E. Radford³ and Neil H. Thomson⁴
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¹ Molecular and Nanoscale Physics Group, School of Physics and Astronomy, University of Leeds, EC Stoner Building, Woodhouse Lane, Leeds, LS2 9JT, UK. ² Molecular and Nanoscale Physics Group, School of Physics and Astronomy, University of Leeds, EC Stoner Building, Woodhouse Lane, Leeds, LS2 9JT, UK. ³ Molecular and Nanoscale Physics Group, School of Physics and Astronomy, University of Leeds, EC Stoner Building, Woodhouse Lane, Leeds, LS2 9JT, UK. ⁴ Molecular and Nanoscale Physics Group, School of Physics and Astronomy, University of Leeds, EC Stoner Building, Woodhouse Lane, Leeds, LS2 9JT, UK.
Source: Protein and Peptide Letters, Volume 13, Issue 3, Mar 2006, p. 261 - 270
DOI: https://doi.org/10.2174/092986606775338498
- Available online: 01 Mar 2006

Abstract

The atomic force microscope (AFM) is a versatile instrument that can be used to image biological samples at nanometre resolution as well as to measure inter and intra-molecular forces in air and liquid environments. This review summarises the use of AFM applied to protein and peptide self-assembly systems involved in amyloid formation. The technical principles of the AFM are outlined and its advantages and disadvantages are highlighted and discussed in the context of the rapidly developing field of amyloid research.

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2006-03-01

2025-05-22

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Article Type: Research Article

Keyword(s): 3D topography; amyloid fibrils; biomimetic environments; contact mode; functional surfaces; self-assembly; Tapping mode; time-lapse microscopy

Amyloid Under the Atomic Force Microscope

Abstract

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