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In situ scanning probe microscopy studies of morphology and growth kinetics in amyloid-peptide fibrillogenesis with custom designed tapping mode and pulsed force mode systems
Luleå University of Technology, Department of Engineering Sciences and Mathematics, Material Science.
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2004 (English)In: Proceedings of 5th Nordic-Baltic Scanning Probe Microscopy Workshop, 2004, 93-95 p.Conference paper, Meeting abstract (Refereed)
Abstract [en]

We have used a commercial Nanoscope II atomic force microscope (AFM) with a custom designedtapping mode (TM) system to in situ monitor amyloid β-peptide aggregation related to Alzheimer’sdisease (AD). The custom tapping mode setup was successfully used to image the real timeaggregation behaviour of the arctic mutation amyloid β-peptide, Aβ(1-40), in vitro in aphysiologically relevant buffer and compare with the behaviour of the normal wild type of theAlzheimer’s amyloid peptide Aβ(1-40) at the same conditions. The investigation revealed distinctdifferences in fibrillogenesis behaviour for the two peptides. Our results demonstrate a previouslysuggested alternative fibrillogenesis pathway, of highly distinct aggregates with orderedmorphology as on-pathway. Moreover, additional investigations using a pulsed force mode (PFM)are under way.

Place, publisher, year, edition, pages
2004. 93-95 p.
Research subject
Chemistry of Interfaces; Fysik; Experimental physics
URN: urn:nbn:se:ltu:diva-35310Local ID: 9cb9e1b4-8f99-450e-ae7c-81bc5342e8bfOAI: diva2:1008563
Nordic-Baltic Scanning Probe Microscopy Workshop : 16/06/2004 - 19/06/2004
Godkänd; 2004; 20120626 (nils)Available from: 2016-09-30 Created: 2016-09-30Bibliographically approved

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