ORGN 729 |
| The fibrils associated with Alzheimer's disease are rich in two forms of the amyloid β peptide (Aβ), comprising residues 1-40 and 1-42. Such fibrils are insoluble and non-crystalline, and are therefore not amenable to study by solution NMR or single-crystal X-ray diffraction. Although detailed atomic-scale structural information is lacking, solid-state NMR has determined that Aβ(1-40) associates via parallel β-sheets. Short fragments of Aβ (5-8 residues) typically provide only limited insight into the process of fibrillogenesis, because the most stable aggregates of such fragments assemble in an antiparallel fashion. We have prepared hairpin-like probe molecules comprising two Aβ fragments linked by an "open crown" poly(ethylene glycol) spacer; the presence of certain metal ions predisposes the peptides to parallel β-sheet formation.
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Asymmetric Reactions, Molecular Recognition, Self Assembly, Bioorganic Chemistry, Process R&D
8:00 PM-10:00 PM, Wednesday, 16 March 2005 Convention Center -- Hall D, Poster
Division of Organic Chemistry |
