The observation of cell membrane damage caused by the interaction between oligomer Amyloid-Beta 1-42 and GM1 gangliosidosis in lipid raft

• Main Authors: Wei Ju Chen, 陳威儒
• Other Authors: C. Chou
• Format: Others
• Published: 2013
• Online Access: http://ndltd.ncl.edu.tw/handle/99444689395390143039

碩士 === 長庚大學 === 光電工程研究所 === 101 === Alzheimer’s disease (AD) is a progressive, neurodegenerative disease. It is characterized by the functional impairment and loss of neurons that results in a progressive decline in memory and other cognitive functions, leading to dementia. Currently without a cure, AD and related disorders will inevitably reach epidemic proportions in a few years. Recent studies have shown that the oligomeric forms of Aβ correlate more strongly with the actual diseased state than either fibril (plaque) or monomers. Thus there must be a mechanism(s) for Aβ oligomers to form, and unfortunately resulting in neurotoxicity. Our working hypothesis is that a highly structured, functional membrane construct, the lipid raft, plays an important role in: a) accumulating Aβ molecules, either in small aggregate forms or influences oligomerization of monomers, and b) membrane integrity is compromised to facilitate osmotic imbalances and/or transport of Aβ oligomers across the membrane.We utilized an ultrasensitive,label-free detection method, the dual-channel paired, surface plasmon wave detector system with ~pM sensitivity, to characterize the interaction between Aβ protein and the supported membrane constructs, starting on lipid bilayer constructs.