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  • Title: A β-hairpin-binding protein for three different disease-related amyloidogenic proteins.
    Author: Shaykhalishahi H, Mirecka EA, Gauhar A, Grüning CS, Willbold D, Härd T, Stoldt M, Hoyer W.
    Journal: Chembiochem; 2015 Feb 09; 16(3):411-4. PubMed ID: 25557164.
    Abstract:
    Amyloidogenic proteins share a propensity to convert to the β-structure-rich amyloid state that is associated with the progression of several protein-misfolding disorders. Here we show that a single engineered β-hairpin-binding protein, the β-wrapin AS10, binds monomers of three different amyloidogenic proteins, that is, amyloid-β peptide, α-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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