Abstract
Alzheimer's disease (AD) is a debilitating disease characterized by the presence of extra-cellular plaques and intra-cellular neurofibrillary tangles (NFTs) in the brain. The major protein component of these plaques is beta amyloid peptide (Aβ), a 40-42 amino acid peptide cleaved from amyloid precursor protein (APP) by β-secretase and a putative γ-secretase. We radioiodinated quinoline derivatives (clioquinol and oxine) and evaluated them as potential amyloid imaging agents based on their ability to cross the blood brain barrier (BBB) and on their selectivity to metal binding sites on amyloid plaques. The uptake of theses tracers in the brains of normal swiss-webster mice was rapid and so was the clearance. Selectivity was demonstrated by higher binding to AD brain homogenates compared to normal brain. Autoradiographic studies demonstrated the localization of the tracers in the plaque regions of the AD brain sections as well as in liver tissue with amyloidosis. Further optimization and evaluations would likely lead to development of these molecules as AD plaque imaging agents.
Original language | English (US) |
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Pages (from-to) | 676-680 |
Number of pages | 5 |
Journal | Nuclear Instruments and Methods in Physics Research, Section B: Beam Interactions with Materials and Atoms |
Volume | 241 |
Issue number | 1-4 |
DOIs | |
State | Published - Dec 2005 |
Keywords
- Alzheimer's disease
- Plaque imaging
- Quinoline derivatives
- Radiolabeled probes
ASJC Scopus subject areas
- Nuclear and High Energy Physics
- Instrumentation