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

Assembly of amyloid-β in association with exosomes

2008년 8월 11일 10시 16분 11초
33P182포 이곳을 클릭하시면 발표코드에 대한 설명을 보실 수 있습니다.
목 <발표Ⅰ>
저자 및
김영규, 박준원1
포항공과대학교 시스템생명공학부, Korea
1포항공과대학교 화학과, Korea
Amyloid-β (Aβ) peptide has been found to cause Alzheimer’s disease, which is the most common neurodegenerative disease. Aβ is not toxic when it is formed from amyloid precursor protein (APP) as a monomer, but becomes toxic when it is assembled into larger structures. In the early days, the fibril was thought to be the most pathogenic species; however, these days, oligomers that are the intermediates are considered to be. Even though many environmental factors such as pH and temperature have been known to influence the transition – that is, assembly - of Aβ from monomers, it is still uncertain how it happens in the brain. Exosomes were reported to carry small amount of Aβ into extracellular space, and ganglioside GM1, which is enriched in the surface of exosomes was shown to be a seed for Aβ fibrillation. Therefore, we suspect that exosomes have a specific role in assembly of Aβ by providing a platform in its early stage. Atomic force microscope (AFM) was chosen as a tool to investigate this hypothesis because of its high spatial resolution enabling the observation of Aβ oligomers whose size are a few nanometers. Moreover, the interaction between Aβ and targeted lipid molecules will be studied with AFM force measurement upon our expertise in this area.