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  • 09월 05일 17시 이후 : 초록수정 불가능, 일정확인 및 검색만 가능

제120회 대한화학회 학술발표회, 총회 및 기기전시회 안내 Investigation of the homo- and hetero-oligomerization of amyloid-β 1-40 and 1-42 using electrospray ionization mass spectrometry

등록일
2017년 8월 31일 11시 09분 27초
접수번호
3132
발표코드
ANAL2.O-35 이곳을 클릭하시면 발표코드에 대한 설명을 보실 수 있습니다.
발표시간
금 10시 : 29분
발표형식
구두발표
발표분야
Analytical Chemistry - Oral Presentation of Young Analytical Chemists II
저자 및
공동저자
Chae Eun Heo, Taesu Choi*, Hugh Inkon Kim*
Department of Chemistry, Korea University, Korea

Self-assembly of amyloid-β peptides (Aβ) has accepted as an important issue, because the final product of the self-assembly (i.e. amyloid fibrils) is highly relevant to the Alzheimer’s disease (AD). Among various Aβ alloforms, Aβ 1-42 (Aβ42) and Aβ 1-40 (Aβ40) are mainly involved in Aβ fibril formation. The self-assembly mechanisms of Aβ42 and Aβ40 are known to be different and Aβ42 and Aβ40 can form hetero-assemblies through their cross-interaction. However, the role of hetero-assemblies of a mixture of Aβ42 and Aβ40 is not yet fully understood. Thus, characterizing the cross-interaction between Aβ42 and Aβ40 is crucial for understanding the role of hetero-assemblies during the fibrillation of mixed Aβ peptides. In this research, we demonstrated the influence of the cross-interaction of Aβ42 and Aβ40 in the early stage of fibrillation. We monitored the fibrillation process of Aβ42, Aβ40 and their 1:1 mixtures using thioflavin T (ThT) assay and electrospray ionization mass spectrometry (ESI-MS). Then, we further investigated the preference for homo- and hetero- oligomerization of Aβ40 and Aβ42 using ion mobility spectrometry (IMS) along with solution small-angle X-ray scattering (SAXS) and molecular dynamics (MD) simulations. Our results suggest that the competitive self-assembly of Aβ42 and Aβ40 plays a pivotal role in disturbing homo-oligomerization of Aβ42 in the early stage of fibrillation.


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