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000203089 1001_ $$0P:(DE-Juel1)167315$$aShaykhalishahi, Hamed$$b0$$ufzj
000203089 245__ $$aA β-Hairpin-Binding Protein for Three Different Disease-Related Amyloidogenic Proteins
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000203089 520__ $$aAmyloidogenic 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.
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000203089 7001_ $$0P:(DE-HGF)0$$aMirecka, Ewa A.$$b1
000203089 7001_ $$0P:(DE-HGF)0$$aGauhar, Aziz$$b2
000203089 7001_ $$0P:(DE-HGF)0$$aGrüning, Clara S. R.$$b3
000203089 7001_ $$0P:(DE-Juel1)132029$$aWillbold, Dieter$$b4$$ufzj
000203089 7001_ $$0P:(DE-HGF)0$$aHärd, Torleif$$b5
000203089 7001_ $$0P:(DE-Juel1)132023$$aStoldt, Matthias$$b6$$ufzj
000203089 7001_ $$0P:(DE-Juel1)166306$$aHoyer, Wolfgang$$b7$$eCorresponding author$$ufzj
000203089 773__ $$0PERI:(DE-600)2020469-3$$a10.1002/cbic.201402552$$gVol. 16, no. 3, p. 411 - 414$$n3$$p411 - 414$$tChemBioChem$$v16$$x1439-4227$$y2015
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