Journal Article

FZJ-2014-02981

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Sequestration of a β-Hairpin for Control of α-Synuclein Aggregation

Mirecka, E. A. ; Shaykhalishahi, H. ; Gauhar, A. ; Akgül, S. ; Lecher, J.FZJ* ; Willbold, D.FZJ* ; Stoldt, M.FZJ* ; Hoyer, W. (Corresponding Author)

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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Contributing Institute(s):

1. Strukturbiochemie (ICS-6)

Research Program(s):

1. 452 - Structural Biology (POF2-452) (POF2-452)

Appears in the scientific report 2014

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Database coverage:
; Current Contents - Life Sciences ; Current Contents - Social and Behavioral Sciences ; JCR ; NCBI Molecular Biology Database ; Nationallizenz ; SCOPUS ; Science Citation Index ; Science Citation Index Expanded ; Thomson Reuters Master Journal List ; Web of Science Core Collection

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