Epitaxial assembly dynamics of mutant amyloid β25-35_N27C fibrils explored with time-resolved scanning force microscopy.

Abstract excerpt

Amyloid β25-35 (Aβ25-35) is a toxic fragment of Alzheimer's beta peptide. We have previously shown that Aβ25-35 fibrils form a trigonally oriented network on mica by epitaxial growth mechanisms. Chemical reactivity can be furnished to the fibril by introducing a cysteine residue (Aβ25-35_N27C) while maintaining oriented assembly properties. Previously we have shown that fibril binding to mica is strongly...

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