| Summary: | 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. Godkänd; 2004; 20120626 (nils)
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