Identifying Biological and Biophysical Features of Different Maturation States of α-Synuclein Amyloid Fibrils
Research output: Contribution to journal › Journal article › Research › peer-review
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.
|Journal||Methods in molecular biology (Clifton, N.J.)|
|Number of pages||24|
|Publication status||Published - 2023|
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- Amyloid fibril maturation, Amyloid polymorphism, Fibril stability, Membrane binding, α-synuclein