Secondary nucleation and elongation occur at different sites on Alzheimer’s amyloid-β aggregates

Tom Scheidt, Urszula Łapińska, Janet R. Kumita, Daniel R. Whiten, David Klenerman, Mark R. Wilson, Samuel I. A. Cohen, 
Sara Linse, Michele Vendruscolo, Christopher M. Dobson, Tuomas P. J. Knowles, and Paolo Arosio

Science Advances, April 2019

A central problem with studying the Aβ aggregate formation is how to interpret macroscopic physical observations determined in experiments. Specifically, in terms of the fundamental microscopic mechanisms that give rise to the overall aggregation behaviour.

However, advances in microfluidic diffusional sizing (MDS) have allowed the authors to show that two molecular chaperones: Brichos domain and Clusterin can inhibit elongation of Aβ fibrils.

Methods rooted in the physical sciences, such as MDS can be applied to analyze the dynamics of such complex systems as the one above. MDS is emerging as a key component in addressing this challenge, enabling us to develop an increasingly detailed molecular picture of amyloid fibril formation.

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