Nucleation of polymorphic amyloid fibrils

Biophysical Journal
Stefan Auer

Abstract

One and the same protein can self-assemble into amyloid fibrils with different morphologies. The phenomenon of fibril polymorphism is relevant biologically because different fibril polymorphs can have different toxicity, but there is no tool for predicting which polymorph forms and under what conditions. Here, we consider the nucleation of polymorphic amyloid fibrils occurring by direct polymerization of monomeric proteins into fibrils. We treat this process within the framework of our newly developed nonstandard nucleation theory, which allows prediction of the concentration dependence of the nucleation rate for different fibril polymorphs. The results highlight that the concentration dependence of the nucleation rate is closely linked with the protein solubility and a threshold monomer concentration below which fibril formation becomes biologically irrelevant. The relation between the nucleation rate, the fibril solubility, the threshold concentration, and the binding energies of the fibril building blocks within fibrils might prove a valuable tool for designing new experiments to control the formation of particular fibril polymorphs.

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Citations

Oct 27, 2015·The Journal of Physical Chemistry. B·L G Rizzi, S Auer
Sep 29, 2015·The Journal of Physical Chemistry. B·Workalemahu M BerhanuUlrich H E Hansmann
Jul 15, 2017·The Journal of Physical Chemistry. B·Stefan Auer
Sep 25, 2017·Israel Journal of Chemistry·Lingyun Zhang, Jeremy D Schmit
Mar 21, 2019·Annual Review of Biomedical Engineering·Jana OgnjenovićSriram Subramaniam

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