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제116회 대한화학회 학술발표회, 총회 및 기기전시회 안내 Development of robust and rapid manner for the inhibitor screening of Amyloid-ß peptide aggregation [우수포스터상]

2015년 8월 27일 16시 47분 04초
BIO.P-209 이곳을 클릭하시면 발표코드에 대한 설명을 보실 수 있습니다.
10월 15일 (목요일) 11:00~12:30
저자 및
이영근, 양승현, 김주환, 강효진, 정상전*
동국대학교 화학과, Korea
Fibrillar aggregates of amyloid-β peptide in the brain is signs of Alzheimer’s disease (AD). Amyloid fiber formation of extracellular amyloid-β peptide deposits is associated with the interactions of high concentration metal ions in the brain. Especially, the rate of amyloid-β aggregation is promoted by high level of zinc ion (Zn2+) that is formed the coordination with histidine and aspartic acid of amyloid-β peptide.[1] Based on this mechanism, development of the inhibitor for preventing amyloid-β peptide aggregation is important. The current aggregates detection and inhibitor screening manner are ELISA, Western blot (WB) and immunoprecipitation (IP).[2, 3] These conventional manners have the limitation such as time consuming, cost and reproducibility. To overcome this weakness, rapid and robust detection manner is designed. Our strategies are based on fluorescence detection manner that observe the increased or decreased fluorescence intensity by amyloid-β aggregate formation as zinc ion concentration. This manner is identified by small molecule Lb-2 that is known to inhibit amyloid-β aggregation in the cell.[4] The strategy may be efficiently applied to drug screening of amyloid-β. Furthermore, we are testing several natural compounds to perform a key role of amyloid-β aggregate inhibition.