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DHPC strongly affects the structure and oligomerization propensity of Alzheimer's Aβ(1-40) peptide

DHPC strongly affects the structure and oligomerization propensity of Alzheimer's Aβ(1-40) peptide

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DAHSE, Kirsten, Megan GARVEY, Michael KOVERMANN, Alexander VOGEL, Jochen BALBACH, Marcus FÄNDRICH, Alfred FAHR, 2010. DHPC strongly affects the structure and oligomerization propensity of Alzheimer's Aβ(1-40) peptide. In: Journal of molecular biology. 403(4), pp. 643-659. ISSN 0022-2836. eISSN 1089-8638. Available under: doi: 10.1016/j.jmb.2010.09.021

@article{Dahse2010-11-05stron-44639, title={DHPC strongly affects the structure and oligomerization propensity of Alzheimer's Aβ(1-40) peptide}, year={2010}, doi={10.1016/j.jmb.2010.09.021}, number={4}, volume={403}, issn={0022-2836}, journal={Journal of molecular biology}, pages={643--659}, author={Dahse, Kirsten and Garvey, Megan and Kovermann, Michael and Vogel, Alexander and Balbach, Jochen and Fändrich, Marcus and Fahr, Alfred} }

<rdf:RDF xmlns:dcterms="http://purl.org/dc/terms/" xmlns:dc="http://purl.org/dc/elements/1.1/" xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" xmlns:bibo="http://purl.org/ontology/bibo/" xmlns:dspace="http://digital-repositories.org/ontologies/dspace/0.1.0#" xmlns:foaf="http://xmlns.com/foaf/0.1/" xmlns:void="http://rdfs.org/ns/void#" xmlns:xsd="http://www.w3.org/2001/XMLSchema#" > <rdf:Description rdf:about="https://kops.uni-konstanz.de/rdf/resource/123456789/44639"> <dc:contributor>Garvey, Megan</dc:contributor> <dc:contributor>Kovermann, Michael</dc:contributor> <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2019-01-21T11:53:18Z</dc:date> <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2019-01-21T11:53:18Z</dcterms:available> <dc:creator>Fahr, Alfred</dc:creator> <dcterms:issued>2010-11-05</dcterms:issued> <dc:creator>Kovermann, Michael</dc:creator> <dc:creator>Dahse, Kirsten</dc:creator> <dc:creator>Garvey, Megan</dc:creator> <dc:creator>Balbach, Jochen</dc:creator> <dc:contributor>Fahr, Alfred</dc:contributor> <dc:contributor>Balbach, Jochen</dc:contributor> <dc:creator>Fändrich, Marcus</dc:creator> <dcterms:isPartOf rdf:resource="https://kops.uni-konstanz.de/rdf/resource/123456789/29"/> <void:sparqlEndpoint rdf:resource="http://localhost/fuseki/dspace/sparql"/> <dcterms:title>DHPC strongly affects the structure and oligomerization propensity of Alzheimer's Aβ(1-40) peptide</dcterms:title> <dc:contributor>Dahse, Kirsten</dc:contributor> <dc:language>eng</dc:language> <foaf:homepage rdf:resource="http://localhost:8080/jspui"/> <dc:contributor>Fändrich, Marcus</dc:contributor> <dc:creator>Vogel, Alexander</dc:creator> <dc:contributor>Vogel, Alexander</dc:contributor> <dcterms:abstract xml:lang="eng">Alzheimer's disease (AD) is thought to depend on the deleterious action of amyloid fibrils or oligomers derived from β-amyloid (Aβ) peptide. Out of various known Aβ alloforms, the 40-residue peptide Aβ(1-40) occurs at highest concentrations inside the brains of AD patients. Its aggregation properties critically depend on lipids, and it was thus proposed that lipids could play a major role in AD. To better understand their possible effects on the structure of Aβ and on the ability of this peptide to form potentially detrimental amyloid structures, we here analyze the interactions between Aβ(1-40) and 1,2-dihexanoyl-sn-glycero-3-phosphocholine (DHPC). DHPC has served, due to its controlled properties, as a major model system for studying general lipid properties. Here, we show that DHPC concentrations of 8 mM or higher exert dramatic effects on the conformation of soluble Aβ(1-40) peptide and induce the formation of β-sheet structure at high levels. By contrast, we find that DHPC concentrations well below the critical micelle concentration present no discernible effect on the conformation of soluble Aβ, although they substantially affect the peptide's oligomerization and fibrillation kinetics. These data imply that subtle lipid-peptide interactions suffice in controlling the overall aggregation properties and drastically accelerate, or delay, the fibrillation kinetics of Aβ peptide in near-physiological buffer solutions.</dcterms:abstract> <dspace:isPartOfCollection rdf:resource="https://kops.uni-konstanz.de/rdf/resource/123456789/29"/> <bibo:uri rdf:resource="https://kops.uni-konstanz.de/handle/123456789/44639"/> </rdf:Description> </rdf:RDF>

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