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Preparation of Crystalline Samples of Amyloid Fibrils and Oligomers
Asher Moshe1, Meytal Landau1, David Eisenberg2
1Department of Biology, Technion-Israel Institute of Technology, Haifa, Israel.
Abstract:
The molecular structures of amyloid fibers and oligomers are required in order to understand and control their formation. Yet, their partially disordered and polymorphic nature hinders structural analyses. Fortunately, short segments from amyloid proteins, which exhibit similar biophysical properties to the full-length proteins, also form fibrils and oligomers and their atomic structures can be determined. Here we describe experimental procedures used to assess fiber-forming capabilities of amyloid peptide segments and their crystallization.
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Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining,...
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