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학술발표회초록보기

초록문의 abstract@kcsnet.or.kr

결제문의 member@kcsnet.or.kr

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  • 02월 19일 10시 이후 : 초록수정 불가능, 일정확인 및 검색만 가능

제121회 대한화학회 학술발표회, 총회 및 기기전시회 안내 Structural characterization of amyloid protein complexes using solution SAXS and ESI-IM-MS

등록일
2018년 2월 3일 20시 00분 55초
접수번호
3624
발표코드
ANAL1-5 이곳을 클릭하시면 발표코드에 대한 설명을 보실 수 있습니다.
발표시간
목 17시 : 00분
발표형식
심포지엄
발표분야
Analytical Chemistry - Recent Advances in Analytical Chemistry I: Optical Sensor Platform Based Nanobio Materials
저자 및
공동저자
Tae Su Choi
Department of Chemistry, Korea University, Korea
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.

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