Monitoring Alzheimer Amyloid Peptide Aggregation by EPR

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SEPKHANOVA, Irina, Malte DRESCHER, Nico J. MEEUWENOORD, Roland W. A. L. LIMPENS, Roman I. KONING, Dmitri V. FILIPPOV, Martina HUBER, 2009. Monitoring Alzheimer Amyloid Peptide Aggregation by EPR. In: Applied Magnetic Resonance. 36(2-4), pp. 209-222. ISSN 0937-9347. eISSN 1613-7507. Available under: doi: 10.1007/s00723-009-0019-1

@article{Sepkhanova2009Monit-1069, title={Monitoring Alzheimer Amyloid Peptide Aggregation by EPR}, year={2009}, doi={10.1007/s00723-009-0019-1}, number={2-4}, volume={36}, issn={0937-9347}, journal={Applied Magnetic Resonance}, pages={209--222}, author={Sepkhanova, Irina and Drescher, Malte and Meeuwenoord, Nico J. and Limpens, Roland W. A. L. and Koning, Roman I. and Filippov, Dmitri V. and Huber, Martina} }

<rdf:RDF xmlns:dcterms="" xmlns:dc="" xmlns:rdf="" xmlns:bibo="" xmlns:dspace="" xmlns:foaf="" xmlns:void="" xmlns:xsd="" > <rdf:Description rdf:about=""> <foaf:homepage rdf:resource="http://localhost:8080/jspui"/> <dspace:isPartOfCollection rdf:resource=""/> <dcterms:available rdf:datatype="">2011-03-22T17:55:04Z</dcterms:available> <dc:creator>Huber, Martina</dc:creator> <dc:contributor>Huber, Martina</dc:contributor> <dspace:isPartOfCollection rdf:resource=""/> <dcterms:title>Monitoring Alzheimer Amyloid Peptide Aggregation by EPR</dcterms:title> <dcterms:isPartOf rdf:resource=""/> <dcterms:issued>2009</dcterms:issued> <dc:creator>Limpens, Roland W. A. L.</dc:creator> <dc:creator>Koning, Roman I.</dc:creator> <dc:creator>Filippov, Dmitri V.</dc:creator> <dcterms:hasPart rdf:resource=""/> <dcterms:bibliographicCitation>Applied Magnetic Resonance ; 36 (2009), 2-4. - S. 209-222</dcterms:bibliographicCitation> <dcterms:isPartOf rdf:resource=""/> <dc:creator>Sepkhanova, Irina</dc:creator> <dc:rights>terms-of-use</dc:rights> <dspace:hasBitstream rdf:resource=""/> <dc:contributor>Meeuwenoord, Nico J.</dc:contributor> <dc:contributor>Drescher, Malte</dc:contributor> <dc:creator>Drescher, Malte</dc:creator> <dc:date rdf:datatype="">2011-03-22T17:55:04Z</dc:date> <dc:contributor>Koning, Roman I.</dc:contributor> <dc:contributor>Limpens, Roland W. A. L.</dc:contributor> <bibo:uri rdf:resource=""/> <dc:creator>Meeuwenoord, Nico J.</dc:creator> <dcterms:rights rdf:resource=""/> <dc:contributor>Sepkhanova, Irina</dc:contributor> <dcterms:abstract xml:lang="eng">Plaques containing the aggregated β-Amyloid (Aβ) peptide in the brain are the main indicators of Alzheimer s disease. Fibrils, the building blocks of plaques, can also be produced in vitro and consist of a regular arrangement of the peptide. The initial steps of fibril formation are not well understood and could involve smaller aggregates (oligomers) of Aβ. Such oligomers have even been implicated as the toxic agents. Here, a method to study oligomers on the time scale of aggregation is suggested. We have labeled the 40 residue Aβ peptide variant containing an N-terminal cysteine (cys-Aβ) with the MTSL [1-oxyl-2,2,5,5-tetramethyl-Δ-pyrroline-3-methyl] methanethiosulfonate spin label (SL-Aβ). Fibril formation in solutions of pure SL-Aβ and of SL-Aβ mixed with Aβ was shown by Congo-red binding and electron microscopy. Continuous-wave 9 GHz electron paramagnetic resonance reveals three fractions of different spin-label mobility: one attributed to monomeric Aβ, one to a multimer (8 15 monomers), and the last one to larger aggregates or fibrils. The approach, in principle, allows detection of oligomers on the time scale of aggregation.</dcterms:abstract> <dc:contributor>Filippov, Dmitri V.</dc:contributor> <dc:language>eng</dc:language> <void:sparqlEndpoint rdf:resource="http://localhost/fuseki/dspace/sparql"/> </rdf:Description> </rdf:RDF>

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