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In vitro analysis o...
In vitro analysis of α-synuclein amyloid formation and cross-reactivity
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- Horvath, Istvan, 1979 (author)
- Chalmers tekniska högskola,Chalmers University of Technology
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- Rocha, Sandra, 1975 (author)
- Chalmers tekniska högskola,Chalmers University of Technology
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- Wittung Stafshede, Pernilla, 1968 (author)
- Chalmers tekniska högskola,Chalmers University of Technology
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(creator_code:org_t)
- 2018-06-08
- 2018
- English.
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In: Methods in Molecular Biology. - New York, NY : Springer New York. - 1940-6029 .- 1064-3745. ; 1779, s. 73-83
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Abstract
Subject headings
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- 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.
Subject headings
- NATURVETENSKAP -- Biologi -- Biofysik (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Biophysics (hsv//eng)
- MEDICIN OCH HÄLSOVETENSKAP -- Medicinsk bioteknologi -- Medicinsk bioteknologi (hsv//swe)
- MEDICAL AND HEALTH SCIENCES -- Medical Biotechnology -- Medical Biotechnology (hsv//eng)
- NATURVETENSKAP -- Biologi -- Bioinformatik och systembiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Bioinformatics and Systems Biology (hsv//eng)
Keyword
- Parkinson’s disease
- Fluorescence
- Thioflavin T
- Electron microscopy
- Amylin
- Type-2 diabetes
- α-Synuclein
- Amyloid
Publication and Content Type
- kap (subject category)
- vet (subject category)
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