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Investigation of MUC1 in Alzheimer's applications

Posted on:2009-02-25Degree:M.SType:Thesis
University:University of Maryland, Baltimore CountyCandidate:Pallikal, James SebastianFull Text:PDF
GTID:2444390005950957Subject:Chemistry
Abstract/Summary:
MUC1 is a highly sialyllated protein which shows potential to interact with the toxic protein β-amyloid (Aβ) of Alzheimer’s disease (AD). We have evaluated the feasibility of using MUC1 fragments as an agent to attenuate Aβ toxicity and bind to Aβ deposits in AD applications. High yield in fragment preparation and small size were verified. MUC1 had no intrinsic toxicity at concentrations tested. The binding affinity of Aβ to the MUC1 fragments was shown to be on the order of 600 nM, which is greater than the binding affinity of Aβ to clustered gangliosides on the cell surface. The addition of MUC1 fragments at low concentrations attenuated Aβ induced cell toxicity. The potential of MUC1 to cross the blood brain barrier was demonstrated. These results signify the potential of using MUC1 fragments in Alzheimer’s applications, and indicate that further work in this area is warranted.
Keywords/Search Tags:MUC1 fragments, Applications, Potential
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