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  • 09월 06일 15시 이후 : 초록수정 불가능, 일정확인 및 검색만 가능

제112회 대한화학회 학술발표회, 총회 및 기기전시회 안내 Development of a Small Molecule Targeting Multiple Facets of Brain Disease

2013년 9월 5일 14시 07분 41초
INOR.P-235 이곳을 클릭하시면 발표코드에 대한 설명을 보실 수 있습니다.
10월 16일 (수요일) 16:00~19:00
저자 및
임미희*, Todd J. Eckroat1, Keith D. Green2, Sylvie Garneau-Tsodikova3, Akiko Kochi4
울산과학기술대학교(UNIST) 나노생명화학공학부, Korea
1Department of Medicinal Chemistry, University of Michigan, USA, United States
2Department of Pharmaceutical Sciences, University of Kentucky, USA, United States
3Department of Pharmaceutical Sciences, University of Kentucky, USA, Canada
4Department of Chemistry, University of Michigan, USA, Japan
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승인 4건
While the etiology of Alzheimer’s disease (AD), a fatal form of dementia, still remains elusive, multiple neuropathological factors, such as misfolded proteins (e.g. Aβ and tau), metal ions, and acetylcholinesterase (AChE) have been proposed to be involved in AD neuropathogenesis. Metal ions and AChE have been observed to be deposited with accumulated Aβ plaques; however, the correlation between all three factors (Aβ, metal ions and AChE) have yet to be elucidated. The interaction between two factors (Aβ and metal ions or AChE), has been studied and reported. Metal binding to Aβ have seen suggested to facilitate Aβ aggregation and generate reactive oxygen species.2 Inhibition of AChE, a serine protease that hydrolyzes the neurotransmitter acetylcholine (ACh), has been shown to temporarily reduce cognitive decline in addition to Aβ aggregation, due to inhibition of the peptide binding to the AChE peripheral site. Therefore, in order to target metal-associated Aβ species and AChE concurrently, a multifunctional small molecule containing bifunctionality (Aβ interaction and metal chelation) and AChE inhibitory activity was designed.4 Herein, the design, synthesis, and characterization of the hybrid will be presented. In addition, we will report the activities of our hybrid toward AChE inhibition with Aβ and/or metal ions as well as metal-free and metal-induced Aβ aggregation in the absence and presence of AChE.