Methods for structural analysis of amyloid fibrils in misfolding diseases

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Abstract

Many proteins and peptides are able to self-assemble in solution in vitro and in vivo to form amyloid-like fibrils. These fibrils share common structural characteristics. In order for a fibril to be characterized as amyloid, it is expected to fit certain criteria including the composition of cross-β. Here we describe how the formation of amyloid fibrils can be characterized in vitro using a variety of methods including circular dichroism and intrinsic tyrosine/tryptophan fluoresence to follow conformational changes; Thioflavin and/or ThS assembly to monitor nucleation and growth; transmission electron microscopy to visualize fibrillar morphology and X-ray fiber diffraction to examine cross-β structure.

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Vadukul, D. M., Al-Hilaly, Y. K., & Serpell, L. C. (2019). Methods for structural analysis of amyloid fibrils in misfolding diseases. In Methods in Molecular Biology (Vol. 1873, pp. 109–122). Humana Press Inc. https://doi.org/10.1007/978-1-4939-8820-4_7

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