Journal Article

FZJ-2015-05124

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png A β-Hairpin-Binding Protein for Three Different Disease-Related Amyloidogenic Proteins

Shaykhalishahi, H.FZJ* ; Mirecka, E. A. ; Gauhar, A. ; Grüning, C. S. R. ; Willbold, D.FZJ* ; Härd, T. ; Stoldt, M.FZJ* ; Hoyer, W. (Corresponding author)FZJ*

2015
Wiley-VCH Weinheim

This record in other databases:      

Please use a persistent id in citations: doi:10.1002/cbic.201402552

Abstract: 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.

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Contributing Institute(s):

1. Strukturbiochemie (ICS-6)

Research Program(s):

1. 553 - Physical Basis of Diseases (POF3-553) (POF3-553)

Appears in the scientific report 2015

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Database coverage:
; BIOSIS Previews ; Current Contents - Life Sciences ; IF < 5 ; JCR ; NCBI Molecular Biology Database ; SCOPUS ; Science Citation Index ; Science Citation Index Expanded ; Thomson Reuters Master Journal List ; Web of Science Core Collection

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