In vitro analysis of α-synuclein amyloid formation and cross-reactivity
Book chapter, 2018

In vitro time-resolved characterization of protein aggregation into amyloid fibers and the effects of other proteins on the aggregation process are fundamentally important measurements to obtain a better understanding of the mechanisms contributing to neurodegeneration, as well as other diseases involving amyloid formation. Here, we describe how to perform in vitro aggregation experiments with α-synuclein, the amyloidogenic protein involved in Parkinson’s disease, including how to assess the starting material, useful experimental/instrumental conditions, as well as how to set up cross-seeding and co-aggregation experiments. The high variability of data reported for in vitro α-synuclein amyloid formation may in part be explained by experimental differences.

Parkinson’s disease

Fluorescence

Thioflavin T

Electron microscopy

Amylin

Type-2 diabetes

α-Synuclein

Amyloid

Author

Istvan Horvath

Chalmers, Biology and Biological Engineering, Chemical Biology

Sandra Rocha

Chalmers, Biology and Biological Engineering, Chemical Biology

Pernilla Wittung Stafshede

Chalmers, Biology and Biological Engineering, Chemical Biology

Methods in Molecular Biology

10643745 (ISSN) 1940-6029 (eISSN)

73-83

Subject Categories

Biophysics

Medical Biotechnology (with a focus on Cell Biology (including Stem Cell Biology), Molecular Biology, Microbiology, Biochemistry or Biopharmacy)

Bioinformatics and Systems Biology

DOI

10.1007/978-1-4939-7816-8_6

More information

Latest update

3/21/2023