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- W2317387050 abstract "Here we present a label-free method for studying the mechanism of surface effects on amyloid aggregation. In this method, spin-coating is used to rapidly dry samples, in a homogeneous manner, after various incubation times. This technique allows the control of important parameters for self-assembly, such as the surface concentration. Atomic force microscopy is then used to obtain high-resolution images of the morphology. While imaging under dry conditions, we show that the morphologies of self-assembled aggregates of a model amyloid-β peptide, Aβ(12-28), are strongly influenced by the local surface concentration. On mica surfaces, where the peptides can freely diffuse, homogeneous, self-assembled protofibrils formed spontaneously and grew longer with longer subsequent incubation. The surface fibrillization rate was much faster than the rates of fibril formation observed in solution, with initiation occurring at much lower concentrations. These data suggest an alternative pathway for amyloid formation on surfaces where the nucleation stage is either bypassed entirely or too fast to measure. This simple preparation procedure for high-resolution atomic force microscopy imaging of amyloid oligomers and protofibrils should be applicable to any amyloidogenic protein species." @default.
- W2317387050 created "2016-06-24" @default.
- W2317387050 creator A5028662408 @default.
- W2317387050 creator A5062311433 @default.
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- W2317387050 date "2014-09-24" @default.
- W2317387050 modified "2023-10-12" @default.
- W2317387050 title "Surface Effects Mediate Self-Assembly of Amyloid-β Peptides" @default.
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- W2317387050 doi "https://doi.org/10.1021/nn5031669" @default.
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