Molecular imaging of amyloid β peptides in mouse brain sections using mass spectrometry
| Autor: | Markus Stoeckli, Karl-Heinz Wiederhold, Matthias Staufenbiel, Dieter Staab, Luca Signor |
|---|---|
| Rok vydání: | 2002 |
| Předmět: |
MALDI imaging
Resolution (mass spectrometry) Amyloid beta Blotting Western Molecular Sequence Data Biophysics Mice Transgenic Peptide Mass spectrometry Sensitivity and Specificity Biochemistry Amyloid beta-Protein Precursor Mice Nuclear magnetic resonance Alzheimer Disease Image Processing Computer-Assisted Animals Frozen Sections Humans Tissue Distribution Amino Acid Sequence Benzothiazoles Molecular Biology Peptide sequence Brain Chemistry chemistry.chemical_classification Amyloid Neuropathies Familial Amyloid beta-Peptides biology Chemistry Brain Reproducibility of Results Cell Biology Thiazoles Amyloid Neuropathy Spectrometry Mass Matrix-Assisted Laser Desorption-Ionization biology.protein Molecular imaging |
| Zdroj: | Analytical Biochemistry. 311:33-39 |
| ISSN: | 0003-2697 |
| Popis: | A method is presented for direct spatial analysis of amyloid beta peptides in biological tissue sections. The technique takes advantage of the very high sensitivity of matrix-assisted laser desorption/ionization mass spectrometry and is implemented on a commercial instrument with modifications to only a few components and the software. With this setup, hundreds of molecular images can be generated simultaneously and within just a few minutes. The current features are an instrumental resolution of 50 microm and a sensitivity down to the attomol range. This new technology is applied to the study of amyloid beta peptide distribution in brain sections from mice, showing features reminiscent of Alzheimer's disease. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Full Text from ScienceDirect