  Using atomic force microscopy (AFM) we investigated the interaction of
amyloid beta (Ab) (1 42) peptide with chemically modified surfaces in order to
better understand the mechanism of amyloid toxicity, which involves interaction
of amyloid with cell membrane surfaces. We compared the structure and density
of Ab fibrils on positively and negatively charged as well as hydrophobic
chemically modified surfaces at physiologically relevant conditions.
