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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},
}