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@ARTICLE{Shaykhalishahi:203089,
author = {Shaykhalishahi, Hamed and Mirecka, Ewa A. and Gauhar, Aziz
and Grüning, Clara S. R. and Willbold, Dieter and Härd,
Torleif and Stoldt, Matthias and Hoyer, Wolfgang},
title = {{A} β-{H}airpin-{B}inding {P}rotein for {T}hree
{D}ifferent {D}isease-{R}elated {A}myloidogenic {P}roteins},
journal = {ChemBioChem},
volume = {16},
number = {3},
issn = {1439-4227},
address = {Weinheim},
publisher = {Wiley-VCH},
reportid = {FZJ-2015-05124},
pages = {411 - 414},
year = {2015},
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.},
cin = {ICS-6},
ddc = {540},
cid = {I:(DE-Juel1)ICS-6-20110106},
pnm = {553 - Physical Basis of Diseases (POF3-553)},
pid = {G:(DE-HGF)POF3-553},
typ = {PUB:(DE-HGF)16},
UT = {WOS:000350136300008},
pubmed = {pmid:25557164},
doi = {10.1002/cbic.201402552},
url = {https://juser.fz-juelich.de/record/203089},
}