This title appears in the Scientific Report :
2014
Please use the identifier:
http://dx.doi.org/10.1002/anie.201309001 in citations.
Sequestration of a β-Hairpin for Control of α-Synuclein Aggregation
Sequestration of a β-Hairpin for Control of α-Synuclein Aggregation
The misfolding and aggregation of the protein α-synuclein (α-syn), which results in the formation of amyloid fibrils, is involved in the pathogenesis of Parkinson's disease and other synucleinopathies. The emergence of amyloid toxicity is associated with the formation of partially folded aggreg...
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Personal Name(s): | Mirecka, E. A |
---|---|
Shaykhalishahi, H. / Gauhar, A. / Akgül, S. / Lecher, Justin / Willbold, Dieter / Stoldt, Matthias / Hoyer, W. (Corresponding Author) | |
Contributing Institute: |
Strukturbiochemie; ICS-6 |
Published in: | Angewandte Chemie / International edition, 53 (2014) 16, S. 4227-4230 |
Imprint: |
Weinheim
Wiley-VCH
2014
|
PubMed ID: |
24623599 |
DOI: |
10.1002/anie.201309001 |
Document Type: |
Journal Article |
Research Program: |
Structural Biology |
Publikationsportal JuSER |
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520 | |a The misfolding and aggregation of the protein α-synuclein (α-syn), which results in the formation of amyloid fibrils, is involved in the pathogenesis of Parkinson's disease and other synucleinopathies. The emergence of amyloid toxicity is associated with the formation of partially folded aggregation intermediates. Here, we engineered a class of binding proteins termed β-wrapins (β-wrap proteins) with affinity for α-synuclein (α-syn). The NMR structure of an α-syn:β-wrapin complex reveals a β-hairpin of α-syn comprising the sequence region α-syn(37-54). The β-wrapin inhibits α-syn aggregation and toxicity at substoichiometric concentrations, demonstrating that it interferes with the nucleation of aggregation.© 2014 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim. | ||
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