Amyloid fibrillation is the supramolecular self-assembly process of amyloid proteins, such as amyloid-β (Aβ), human islet amyloid polypeptide (hIAPP), and α-synuclien (αSyn). Amyloid fibril, the final product of amyloid fibrillation, is involved to the pathologic functions of neurodegenerative diseases. Thus, unraveling the fibrillation mechanism is crucial for suggesting the toxic mechanism by amyloid fibrils and a therapeutic strategy for reducing the formation of cytotoxic aggregates. Generally, the fibrillation is initiated through the structural transition of the amyloid proteins. The conformational change in protein structures commonly destabilizes intra-molecular interaction of the proteins, while inducing inter-molecular interaction between destabilized proteins. Thus, to study the fibrillation mechanism, understanding the structural transition of amyloid proteins and its correlation with their amyloid fibrillation is a major priority. Here, I will present our recent approaches in the structural characterization of amyloid proteins complexes and their effect on the fibrillation processes.<br/>

Investigating structural transitions of amyloid proteins in the early stage of aggregations using ion mobility mass spectrometry (IM-MS) and small-angle X-ray scattering (SAXS)

256th National Meeting (2018)

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