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Methods Mol Biol. 2016;1345:133-50. doi: 10.1007/978-1-4939-2978-8_9.

Formation and Characterization of α-Synuclein Oligomers.

Author information

1
Department of Molecular Biology, Center for Insoluble Protein Structures (inSPIN), Interdisciplinary Nanoscience Center (iNANO), Aarhus University, Gustav Wieds Vej 14, 8000, Aarhus C, Denmark.
2
Department of Clinical Neuroscience, Karolinska Institutet, Stockholm, Sweden, 171 77.
3
Department of Protein Biophysics and Formulation, Novo Nordisk A/S, 2760, Måløv, Denmark.
4
Department of Molecular Biology, Center for Insoluble Protein Structures (inSPIN), Interdisciplinary Nanoscience Center (iNANO), Aarhus University, Gustav Wieds Vej 14, 8000, Aarhus C, Denmark. dao@inano.au.dk.

Abstract

The aggregation of α-synuclein (αSN) into oligomeric structures has received increasing interest during the last 10-15 years. The oligomers' potential involvement in Parkinson's disease makes them a promising therapeutic target. Therefore reproducible protocols to prepare and analyze oligomers are very important to allow direct comparison of results obtained by different research groups. In this chapter we present one established method to obtain αSN oligomers from a monomeric ensemble in a relatively easy manner. Also, we briefly discuss a selection of biophysical methods which allow for a quick characterization of oligomer purity and structure.

KEYWORDS:

Aggregation; Biophysics; Chromatography; Oligomer; Protein; Purification; α-synuclein

PMID:
26453210
DOI:
10.1007/978-1-4939-2978-8_9
[Indexed for MEDLINE]

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