This title appears in the Scientific Report :
2015
Please use the identifier:
http://dx.doi.org/10.1002/cbic.201402552 in citations.
A β-Hairpin-Binding Protein for Three Different Disease-Related Amyloidogenic Proteins
A β-Hairpin-Binding Protein for Three Different Disease-Related Amyloidogenic Proteins
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 amyloidogen...
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Personal Name(s): | Shaykhalishahi, Hamed |
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Mirecka, Ewa A. / Gauhar, Aziz / Grüning, Clara S. R. / Willbold, Dieter / Härd, Torleif / Stoldt, Matthias / Hoyer, Wolfgang (Corresponding author) | |
Contributing Institute: |
Strukturbiochemie; ICS-6 |
Published in: | ChemBioChem, 16 (2015) 3, S. 411 - 414 |
Imprint: |
Weinheim
Wiley-VCH
2015
|
PubMed ID: |
25557164 |
DOI: |
10.1002/cbic.201402552 |
Document Type: |
Journal Article |
Research Program: |
Physical Basis of Diseases |
Publikationsportal JuSER |
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. |