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DC Field | Value | Language |
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dc.contributor.author | Högen, Tobias | - |
dc.contributor.author | Levin, Johannes | - |
dc.contributor.author | Schmidt, Felix | - |
dc.contributor.author | Caruana Grech Perry, Mario | - |
dc.contributor.author | Vassallo, Neville | - |
dc.contributor.author | Kretzschmar, Hans A. | - |
dc.contributor.author | Bötzel, Kai | - |
dc.contributor.author | Kamp, Frits | - |
dc.contributor.author | Giese, Armin | - |
dc.date.accessioned | 2019-08-28T10:22:43Z | - |
dc.date.available | 2019-08-28T10:22:43Z | - |
dc.date.issued | 2012 | - |
dc.identifier.citation | Högen, T., Levin, J., Schmidt, F., Caruana, M., Vassallo, N., Kretzschmar, H.,...Giese, A. (2012). Two different binding modes of α-synuclein to lipid vesicles depending on its aggregation state. Biophysical Journal, 102(7), 1646-1655. | en_GB |
dc.identifier.uri | https://www.um.edu.mt/library/oar/handle/123456789/45983 | - |
dc.description.abstract | Aggregation of α-synuclein is involved in the pathogenesis of Parkinson's disease (PD). Studies of in vitro aggregation of α-synuclein are rendered complex because of the formation of a heterogeneous population of oligomers. With the use of confocal single-molecule fluorescence techniques, we demonstrate that small aggregates (oligomers) of α-synuclein formed from unbound monomeric species in the presence of organic solvent (DMSO) and iron (Fe 3+) ions have a high affinity to bind to model membranes, regardless of the lipid-composition or membrane curvature. This binding mode contrasts with the well-established membrane binding of α-synuclein monomers, which is accompanied with α-helix formation and requires membranes with high curvature, defects in the lipid packing, and/or negatively charged lipids. Additionally, we demonstrate that membrane-bound α-synuclein monomers are protected from aggregation. Finally, we identified compounds that potently dissolved vesicle-bound α-synuclein oligomers into monomers, leaving the lipid vesicles intact. As it is commonly believed that formation of oligomers is related PD progression, such compounds may provide a promising strategy for the design of novel therapeutic drugs in Parkinson's disease. | en_GB |
dc.language.iso | en | en_GB |
dc.publisher | Elsevier | en_GB |
dc.rights | info:eu-repo/semantics/openAccess | en_GB |
dc.subject | Alpha-synuclein -- Oligomerization | en_GB |
dc.subject | Parkinson's disease -- Chemotherapy | en_GB |
dc.subject | Parkinson's disease -- Pathogenesis | en_GB |
dc.subject | Parkinson's disease -- Pathophysiology | en_GB |
dc.subject | Phospholipids | en_GB |
dc.title | Two different binding modes of α-synuclein to lipid vesicles depending on its aggregation state | en_GB |
dc.type | article | en_GB |
dc.rights.holder | The copyright of this work belongs to the author(s)/publisher. The rights of this work are as defined by the appropriate Copyright Legislation or as modified by any successive legislation. Users may access this work and can make use of the information contained in accordance with the Copyright Legislation provided that the author must be properly acknowledged. Further distribution or reproduction in any format is prohibited without the prior permission of the copyright holder. | en_GB |
dc.description.reviewed | peer-reviewed | en_GB |
dc.identifier.doi | 10.1016/j.bpj.2012.01.059 | - |
dc.publication.title | Biophysical Journal | en_GB |
Appears in Collections: | Scholarly Works - FacM&SPB |
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Two_different_binding_modes_of_α-synuclein_to_lipid_vesicles_depending_on_its_aggregation_state_2012.pdf | 1.23 MB | Adobe PDF | View/Open |
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