This title appears in the Scientific Report : 2014 

Sequestration of a β-Hairpin for Control of α-Synuclein Aggregation
Mirecka, E. A
Shaykhalishahi, H. / Gauhar, A. / Akgül, S. / Lecher, Justin / Willbold, Dieter / Stoldt, Matthias / Hoyer, W. (Corresponding Author)
Strukturbiochemie ; ICS-6
Angewandte Chemie / International edition, 53 (2014) 16, S. 4227-4230
Weinheim Wiley-VCH 2014
24623599
10.1002/anie.201309001
Journal Article
Structural Biology
Please use the identifier: http://dx.doi.org/10.1002/anie.201309001 in citations.
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.