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  • 08월 28일 16시 이후 : 초록수정 불가능, 일정확인 및 검색만 가능

Biological tactics to control in vitro beta-amyloid aggregation

등록일
2008년 8월 12일 09시 27분 17초
접수번호
0989
발표코드
33P217포 이곳을 클릭하시면 발표코드에 대한 설명을 보실 수 있습니다.
발표시간
목 <발표Ⅰ>
발표형식
포스터
발표분야
생명화학
저자 및
공동저자
김혜연, 김영수, 김동진
한국과학기술연구원 케모인포메틱스연구단, Korea
Amyloid beta (Aβ) is a main constituent of amyloid plaques in the brains of Alzheimer's disease (AD) patients, existing in several states; monomers, oligomers, and fibrils. Oligomers are known to be the most toxic form, while the monomer and the fibril forms are less. Therefore, it is critical to separate or visualize oligomers from the amyloid mixture for AD researchers. In current assay systems employing Aβ to screen aggregation inhibitors or imaging probes, as cure/diagnosis tools for AD, Aβ(1-42) is often used in vitro, because Aβ(1-42) monomers aggregate into fibrils in less than two hours while it takes about seven days to deposit Aβ(1-40) fibrils. However, the advantage of Aβ(1-42), the quick aggregation property, also accompanies difficulties to study the oligomer state of the amyloidosis. On the other hand, Aβ(1-40), which is the most frequent form of Aβ produced following enzymatic cleavage of amyloid precursor protein, is reported to take a important role in initiation of amyloidosis in AD brains. Thus, Aβ(1-40) can be beneficial by adopting its relatively slow oligomerization property. Here we report a new in vitro assay system established at KIST which can control aggregation transitions from monomers to oligomers and fibrils by employing various biological buffers and SDS-PAGE with Photoinduced Cross-Linking of Unmodified Proteins (PICUP) protocols. These buffers are categorized into three basic structures having a scaffold such glycine, taurine, and tramiprosate, known as an inhibitor for Aβ oligomerization. Depending on functional moieties of buffer’s N-terminus, oligomerization of Aβ can be accelerated or inhibited. Our system can offer significant savings in time and cost for the study of the Aβ oligomerization, where no high throughput assay is available, and the new buffer assay method can contribute to the advancement of basic experimental protocol for the development of AD treatments and imaging probes targeting assembled Aβ in AD brains.

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