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@ARTICLE{Zhang:864099,
author = {Zhang, Tao and Nagel-Steger, Luitgard and Willbold, Dieter},
title = {{S}olution-{B}ased {D}etermination of {D}issociation
{C}onstants for the {B}inding of {A}β42 to {A}ntibodies},
journal = {ChemistryOpen},
volume = {8},
number = {7},
issn = {2191-1363},
address = {Weinheim},
publisher = {Wiley-VCH-Verl.},
reportid = {FZJ-2019-04002},
pages = {989 - 994},
year = {2019},
abstract = {Amyloid β‐peptides (Aβ) play a major role in the
pathogenesis of Alzheimer's disease. Therefore, numerous
monoclonal antibodies against Aβ have been developed for
basic and clinical research. The present study applied
fluorescence based analytical ultracentrifugation and
microscale thermophoresis to characterize the interaction
between Aβ42 monomers and three popular, commercially
available antibodies, namely 6E10, 4G8 and 12F4. Both
methods allowed us to analyze the interactions at low
nanomolar concentrations of analytes close to their
dissociation constants (KD) as required for the study of
high affinity interactions. Furthermore, the low
concentrations minimized the unwanted self‐aggregation of
Aβ. Our study demonstrates that all three antibodies bind
to Aβ42 monomers with comparable affinities in the low
nanomolar range. KD values for Aβ42 binding to 6E10 and 4G8
are in good agreement with formerly reported values from SPR
studies, while the KD for 12F4 binding to Aβ42 monomer is
reported for the first time.},
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},
pubmed = {pmid:31367507},
UT = {WOS:000477965100019},
doi = {10.1002/open.201900167},
url = {https://juser.fz-juelich.de/record/864099},
}