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  • 09월 20일 16시 이후 : 초록수정 불가능, 일정확인 및 검색만 가능

제126회 대한화학회 학술발표회 및 총회 Kinetic modulation of Amyloid-β through its point mutation by structure-based design

2020년 9월 9일 22시 17분 05초
ANAL1.O-11 이곳을 클릭하시면 발표코드에 대한 설명을 보실 수 있습니다.
화 09시 : 40분
Analytical Chemistry - Oral Presentation of Young Analytical Chemists I
저자 및
Dongjoon Im, Chae Eun Heo, MyungKook Son, Chae Ri Park, Sooyeon Chae, Min Ji Kim1, Hugh I. Kim*
Department of Chemistry, Korea University, Korea
1Chemistry, Korea University, Korea
Modulating the formation process of amyloid-β fibril, especially kinetically delaying its early onset, is an applicable solution for Alzheimer's disease patients along with early diagnosis. The aggregates of Amyloid-β (Aβ) fibrils which are commonly observed in the brain of the Alzheimer's disease patients are considered to be closely related to the pathogenesis of the disease. Amyloid-β peptides with different number of residues may look alike but clearly have different physical properties. The peptides consisting of 40 and 42 amino acids, the two most dominant species, only differ in two amino acids of the N-terminal which is what provokes the difference of the entire morphology of their fibril structure, accelerated fibrillation of Aβ 42 to Aβ 40 as well as other properties. Since Aβ 42 to Aβ 40 ratio is found to be higher in patients compared to non-patients, we suggested the distinct physical properties of Aβ 42 to act as key factors in making it prone to self-assembly. In this study, we rationally designed mutant peptides with various point mutations based on their structure and physical properties. Designed mutant peptides have not only shown suppressed self-assembly, but also slowed down fibrillation process when mixed with wild type Amyloid-β (1-42).