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| Home > Publications database > Sequestration of a β-Hairpin for Control of α-Synuclein Aggregation |
| Home > Publications database > Sequestration of a β-Hairpin for Control of α-Synuclein Aggregation |
| Journal Article | FZJ-2014-02981 |
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2014
Wiley-VCH
Weinheim
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Please use a persistent id in citations: doi:10.1002/anie.201309001
Abstract: 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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