|
Type |
Symposium |
Area |
Recent Advances in Analytical Chemistry I: Optical Sensor Platform Based Nanobio Materials |
Room No. |
Room 201A |
Time |
THU 17:00-: |
Code |
ANAL1-5 |
Subject |
Structural characterization of amyloid protein complexes using solution SAXS and ESI-IM-MS |
Authors |
Tae Su Choi Department of Chemistry, Korea University, Korea |
Abstract |
Various amyloid proteins (e.g. amyloid-β (Aβ) and α-Synuclein (αSyn)) self-assemble to β-sheet rich, fibrillar aggregates. The formation of Aβ and αSyn fibrils has been linked to the onset and progress of Alzheimer’s disease (AD) and Parkinson’s disease (PD). It has been suggested that diverse biomolecules are involved in the structural transition of Aβ and αSyn, thereby suppressing or promoting the amyloid self-assembly. However, their molecular mechanism and impacts on cell environment are unclear yet. Thus, unraveling the role of biomolecules in Aβ and αSyn structures is the primary step forward understanding the pathologies of AD and PD. In this seminar, I will discuss two examples: human serum albumin (HSA)–Aβ and αSyn–Cu(II) complexes. Firstly, the quantitative structural analysis of two complexes will be presented using small-angle X-ray scattering (SAXS) and ion mobility-mass spectrometry (IM-MS). Then, the molecular mechanism of the amyloid self-assembly by these complexes and its impact on cell responses will be further discussed. |
E-mail |
choitaesu@korea.ac.kr |
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