%0 Journal Article
%A Shaykhalishahi, Hamed
%A Mirecka, Ewa A.
%A Gauhar, Aziz
%A Grüning, Clara S. R.
%A Willbold, Dieter
%A Härd, Torleif
%A Stoldt, Matthias
%A Hoyer, Wolfgang
%T A β-Hairpin-Binding Protein for Three Different Disease-Related Amyloidogenic Proteins
%J ChemBioChem
%V 16
%N 3
%@ 1439-4227
%C Weinheim
%I Wiley-VCH
%M FZJ-2015-05124
%P 411 - 414
%D 2015
%X Amyloidogenic proteins share a propensity to convert to the b-structure-rich amyloid state that is associated with the progression of several protein-misfolding disorders. Here we show that a single engineered b-hairpin-binding protein, the bwrapin AS10, binds monomers of three different amyloidogenic proteins, that is, amyloid-b peptide, a-synuclein, and islet amyloid polypeptide, with sub-micromolar affinity. AS10 binding inhibits the aggregation and toxicity of all three proteins. The results demonstrate common conformational preferences and related binding sites in a subset of the amyloidogenic proteins. These commonalities enable the generation of multispecific monomer-binding agents.
%F PUB:(DE-HGF)16
%9 Journal Article
%U <Go to ISI:>//WOS:000350136300008
%$ pmid:25557164
%R 10.1002/cbic.201402552
%U https://juser.fz-juelich.de/record/203089