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Engineered binding proteins to amyloidogenic peptides and proteins


The aggregation of proteins into amyloid fibril deposits is a pathological feature of various diseases, including nearly every major neurodegenerative disease such as Alzheimer and Parkinson. We develop, characterize, and apply engineered binding proteins to amyloid-forming proteins, in order to elucidate and modulate protein aggregation reactions. For this purpose, we employ a wide range of techniques in the area of biophysics, biochemistry, and molecular biology.

Beta-wrapins: Engineered binding proteins to amyloid-forming proteins
We generate small binding proteins, termed beta-wrapins, with affinities for key proteins involved in protein misfolding disorders, including alpha-synuclein (Parkinson), tau (Alzheimer), islet amyloid polypeptide (Type 2 diabetes), and amyloid-beta (Alzheimer). Beta-wrapins inhibit aggregation and toxicity of the target proteins. Beta-wrapins act by interfering with the nucleation of aggregation and shifting the equilibrium to the monomeric, soluble state.

Beta-hairpin motifs for molecular recognition of amyloid-forming proteins
Amyloid-forming proteins locally adopt beta-structure upon binding to beta-wrapins. For example, we have identified a beta-hairpin motif in alpha-synuclein. The beta-hairpin is formed in a sequence region that is critical for pathogenesis of Parkinson disease, containing most of the reported disease-related point mutations.

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Amyloid-Proteinablagerungen sind ein pathologisches Merkmal fast aller neurodegenerativer Erkrankungen wie zum Beispiel Alzheimer und Parkinson. Wir erforschen den Mechanismus der Amyloidbildung und untersuchen, wie er beeinflusst werden kann. Dazu setzen wir vielfältige biophysikalische, biochemische und molekularbiologische Methoden ein.

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