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  • 02월 19일 23시 이후 : 초록수정 불가능, 일정확인 및 검색만 가능

제119회 대한화학회 학술발표회, 총회 및 기기전시회 Characterization of heterogeneous oligomerization of amyloid-β 1-40 and 1-42 using electrospray ionization mass spectrometry

2017년 2월 17일 16시 54분 52초
ANAL2.O-48 이곳을 클릭하시면 발표코드에 대한 설명을 보실 수 있습니다.
금 10시 : 42분
분석화학 - Oral Presentation of Young Analytical Chemists Ⅱ
저자 및
허채은, 김준곤*
고려대학교 화학과, Korea
Amyloid fibrillation of amyloid-β (Aβ) peptides has been accepted as the main cause of Alzheimer’s disease (AD). Aβ40 is the most abundant form in Aβ peptides, while Aβ42 is highly relevant to the progress of AD. The ratio of Aβ40:Aβ42 in human brain is approximately 9:1, but the ratio of Aβ42 is increased in the brains of patients with AD. Since Aβ42 is more aggregation-prone than Aβ40, amyloid fibrillation of Aβ peptides can be promoted when increasing the ratio of Ab42. Additionally, it has been reported that the high ratio of Aβ40 inhibits the aggregation of Aβ42. However, the molecular interaction between Aβ40 and Aβ42 during the inhibition of Aβ42 fibrillation is still unclear. In this research, we demonstrate the role of Aβ40 during the fibrillation process of Aβ42. 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 changes in gas-phase structures of homo- and hetero- oligomers of Aβ40 and Aβ42 using ion mobility spectrometry (IMS) combined with ESI-MS. Our results suggest that Aβ40 delays the nucleation process of Aβ42 by forming the hetero-oligomers, and overall rates in the fibrillation kinetics are decreased.