Different Structural Conformers of Monomeric α-Synuclein Identified after Lyophilizing and Freezing.

ABSTRACT: Understanding the mechanisms behind amyloid protein aggregation in diseases, such as Parkinson's and Alzheimer's disease, is often hampered by the reproducibility of in vitro assays. Yet, understanding the basic mechanisms of protein misfolding is essential for the development of novel therapeutic strategies. We show here, that for the amyloid protein α-synuclein (aSyn), a protein involved in Parkinson's disease (PD), chromatographic buffers and storage conditions can significantly interfere with the overall structure of the protein and thus affect protein aggregation kinetics. We apply several biophysical and biochemical methods, including size exclusion chromatography (SEC), dynamic light scattering (DLS), and atomic force microscopy (AFM), to characterize the high molecular weight confo

SUBMITTER: Stephens AD 

PROVIDER: S-EPMC6047843 | biostudies-literature | 2018 Jun

REPOSITORIES: biostudies-literature