Thesis advisor: Daniel Kirschner / Alzheimer's disease is the leading cause of dementia in the United States. The neurodegenerative condition of this disease correlates with the formation in the brain of plaques consisting of insoluble protein aggregates, termed amyloid. The aggregates are caused by the misfolding of amyloid β, a 40—42 amino acid polypeptide that is naturally occurring in all humans. One approach to preventing the amyloid cytotoxicity is to prevent the formation of plaques altogether. Many types of inhibitors have been tested for their therapeutic value, including substituted peptide strands. In this study, the inhibitory potential of two such peptides was tested: methylated peptides and nitrile-substituted peptides. Aβ(16-22) was used for its fiber-forming properties, and x-ray diffraction and transmission electron microscopy were used to assess the extent of fibrillogenesis. The methylated peptide effectively inhibited fiber formation as previously recorded, and the cyanophenylalanine derivatives did not form fibers. The latter experiment provided insight on the structural and folding properties of Aβ more than its possible inhibitory potential. / Submitted to: Boston College. College of Arts and Sciences. / Discipline: Biology. / Discipline: College Honors Program.
| Identifer | oai:union.ndltd.org:BOSTON/oai:dlib.bc.edu:bc-ir_102432 |
| Date | January 2008 |
| Creators | Gleason, Katherine |
| Publisher | Boston College |
| Source Sets | Boston College |
| Language | English |
| Detected Language | English |
| Type | Text, thesis |
| Format | electronic, application/pdf |
| Rights | Copyright is held by the author, with all rights reserved, unless otherwise noted. |
Page generated in 0.0023 seconds