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.

  • Publications and resources

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    • Publication25 July 2019

      Microfluidic diffusional sizing (MDS) in the literature

      Document referencing all the publications where microfluidic diffusional sizing (MDS) has been used.

    • Infographic11 July 2019

      Researching therapies for Alzheimer’s Disease

      In this infographic, we break down all the failures of potential therapies that were tested to treat Alzheimer's Disease. This includes a cost and percentage breakdown of the clinical phases in which these therapies failed in as well as statistics for world-wide Alzherimer's Disease epidemiology.

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