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

• Main Authors: Hellberg, Magnus, Norlin, Nils, Olevik, David, Almqvist, Nils, Antzutkin, Oleg
• Format: Conference Object
• Language: English
• Published: Luleå tekniska universitet, Materialvetenskap 2004
• Subjects: Physical Chemistry; Fysikalisk kemi; Other Physics Topics; Annan fysik; Arctic; Nils
• Online Access: http://urn.kb.se/resolve?urn=urn:nbn:se:ltu:diva-35310

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)