TY  - JOUR
AU  - Mirecka, E. A
AU  - Shaykhalishahi, H.
AU  - Gauhar, A.
AU  - Akgül, S.
AU  - Lecher, Justin
AU  - Willbold, Dieter
AU  - Stoldt, Matthias
AU  - Hoyer, W.
TI  - Sequestration of a β-Hairpin for Control of α-Synuclein Aggregation
JO  - Angewandte Chemie / International edition
VL  - 53
IS  - 16
SN  - 0570-0833
CY  - Weinheim
PB  - Wiley-VCH
M1  - FZJ-2014-02981
SP  - 4227-4230
PY  - 2014
AB  - 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.
LB  - PUB:(DE-HGF)16
C6  - pmid:24623599
UR  - <Go to ISI:>//WOS:000338968700022
DO  - DOI:10.1002/anie.201309001
UR  - https://juser.fz-juelich.de/record/153349
ER  -