Simultaneous IR-spectroscopic observation of α-synuclein, lipids, and solvent reveals an alternative membrane-induced oligomerization pathway
| Type of Publication: | Journal article |
| Publication status: | Published |
| URI (citable link): | http://nbn-resolving.de/urn:nbn:de:bsz:352-2-1eodq8f5g6c7y3 |
| Author: | Fallah, Mohammad A; Gerding, Hanne R.; Scheibe, Christian; Drescher, Malte; Karreman, Christiaan; Schildknecht, Stefan; Leist, Marcel; Hauser, Karin |
| Year of publication: | 2017 |
| Published in: | ChemBioChem ; 18 (2017), 23. - pp. 2312-2316. - ISSN 1439-4227. - eISSN 1439-7633 |
| Pubmed ID: | 28980756 |
| DOI (citable link): | https://dx.doi.org/10.1002/cbic.201700355 |
| Summary: |
The intrinsically disordered protein α-synuclein (αS), a known pathogenic factor for Parkinson's disease, can adopt defined secondary structures when interacting with membranes or during fibrillation. The αS-lipid interaction and the implications of this process for aggregation and damage to membranes are still poorly understood. Therefore, we established a label-free infrared (IR) spectroscopic approach to simultaneously monitor αS conformation and membrane integrity. IR showed its unique sensitivity for identifying distinct α-structured aggregates. A comparative study of wildtype αS and the naturally occurring splicing variant αS Δexon3 yielded new insights into the membrane's capability of altering aggregation pathways.
|
| Subject (DDC): | 570 Biosciences, Biology |
| Link to License: | In Copyright |
| Bibliography of Konstanz: | Yes |
Cite This
Files in this item
![[PDF]](/themes/Kops/images/mimes/pdf.png "PDF file"){kind=small}
FALLAH, Mohammad A, Hanne R. GERDING, Christian SCHEIBE, Malte DRESCHER, Christiaan KARREMAN, Stefan SCHILDKNECHT, Marcel LEIST, Karin HAUSER, 2017. Simultaneous IR-spectroscopic observation of α-synuclein, lipids, and solvent reveals an alternative membrane-induced oligomerization pathway. In: ChemBioChem. 18(23), pp. 2312-2316. ISSN 1439-4227. eISSN 1439-7633. Available under: doi: 10.1002/cbic.201700355
@article{Fallah2017-12-05Simul-40331, title={Simultaneous IR-spectroscopic observation of α-synuclein, lipids, and solvent reveals an alternative membrane-induced oligomerization pathway}, year={2017}, doi={10.1002/cbic.201700355}, number={23}, volume={18}, issn={1439-4227}, journal={ChemBioChem}, pages={2312--2316}, author={Fallah, Mohammad A and Gerding, Hanne R. and Scheibe, Christian and Drescher, Malte and Karreman, Christiaan and Schildknecht, Stefan and Leist, Marcel and Hauser, Karin} }
<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/123456789/40331"> <dc:rights>terms-of-use</dc:rights> <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2017-10-13T11:26:09Z</dcterms:available> <dspace:hasBitstream rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/40331/1/Fallah_2-1eodq8f5g6c7y3.pdf"/> <dcterms:hasPart rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/40331/1/Fallah_2-1eodq8f5g6c7y3.pdf"/> <dc:contributor>Fallah, Mohammad A</dc:contributor> <void:sparqlEndpoint rdf:resource="http://localhost/fuseki/dspace/sparql"/> <dc:creator>Leist, Marcel</dc:creator> <dc:language>eng</dc:language> <dcterms:rights rdf:resource="https://rightsstatements.org/page/InC/1.0/"/> <dc:creator>Gerding, Hanne R.</dc:creator> <dspace:isPartOfCollection rdf:resource="https://kops.uni-konstanz.de/rdf/resource/123456789/28"/> <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2017-10-13T11:26:09Z</dc:date> <dcterms:abstract xml:lang="eng">The intrinsically disordered protein α-synuclein (αS), a known pathogenic factor for Parkinson's disease, can adopt defined secondary structures when interacting with membranes or during fibrillation. The αS-lipid interaction and the implications of this process for aggregation and damage to membranes are still poorly understood. Therefore, we established a label-free infrared (IR) spectroscopic approach to simultaneously monitor αS conformation and membrane integrity. IR showed its unique sensitivity for identifying distinct α-structured aggregates. A comparative study of wildtype αS and the naturally occurring splicing variant αS Δexon3 yielded new insights into the membrane's capability of altering aggregation pathways.</dcterms:abstract> <dcterms:issued>2017-12-05</dcterms:issued> <foaf:homepage rdf:resource="http://localhost:8080/jspui"/> <dc:creator>Karreman, Christiaan</dc:creator> <dc:contributor>Karreman, Christiaan</dc:contributor> <dc:creator>Fallah, Mohammad A</dc:creator> <dc:contributor>Schildknecht, Stefan</dc:contributor> <dc:creator>Schildknecht, Stefan</dc:creator> <dc:contributor>Leist, Marcel</dc:contributor> <dc:contributor>Gerding, Hanne R.</dc:contributor> <bibo:uri rdf:resource="https://kops.uni-konstanz.de/handle/123456789/40331"/> <dcterms:title>Simultaneous IR-spectroscopic observation of α-synuclein, lipids, and solvent reveals an alternative membrane-induced oligomerization pathway</dcterms:title> <dc:creator>Scheibe, Christian</dc:creator> <dcterms:isPartOf rdf:resource="https://kops.uni-konstanz.de/rdf/resource/123456789/28"/> <dc:contributor>Hauser, Karin</dc:contributor> <dc:creator>Drescher, Malte</dc:creator> <dc:contributor>Scheibe, Christian</dc:contributor> <dc:contributor>Drescher, Malte</dc:contributor> <dc:creator>Hauser, Karin</dc:creator> </rdf:Description> </rdf:RDF>
Downloads since Oct 13, 2017 (Information about access statistics)
| Fallah_2-1eodq8f5g6c7y3.pdf | 127 |
This item appears in the following Collection(s)
Search KOPS
Browse
My Account
