Identifying Biological and Biophysical Features of Different Maturation States of α-Synuclein Amyloid Fibrils

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Protein aggregates, hereunder amyloid fibrils, can undergo a maturation process, whereby early formed aggregates undergo a structural and physicochemical transition leading to more mature species. In the case of amyloid-related diseases, such maturation confers distinctive biological properties of the aggregates, which may account for a range of diverse pathological subtypes. Here, we present a protocol for the preparation of α-synuclein amyloid fibrils differing in the level of their maturation. We utilize widely accessible biophysical techniques to characterize the structure and morphology and a simple thermal treatment procedure to test their thermodynamic stability. Their biological properties are probed by means of binding to native plasma membrane sheets originating from mammalian cell lines.

Original languageEnglish
JournalMethods in molecular biology (Clifton, N.J.)
Pages (from-to)321-344
Number of pages24
Publication statusPublished - 2023

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Publisher Copyright:
© 2023. Springer Science+Business Media, LLC, part of Springer Nature.

    Research areas

  • Amyloid fibril maturation, Amyloid polymorphism, Fibril stability, Membrane binding, α-synuclein

ID: 324823266