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@ARTICLE{Girelli:901872,
      author       = {Girelli, Anita and Beck, Christian and Bäuerle, Famke and
                      Matsarskaia, Olga and Maier, Ralph and Zhang, Fajun and Wu,
                      Baohu and Lang, Christian and Czakkel, Orsolya and Seydel,
                      Tilo and Schreiber, Frank and Roosen-Runge, Felix},
      title        = {{M}olecular {F}lexibility of {A}ntibodies {P}reserved
                      {E}ven in the {D}ense {P}hase after {M}acroscopic {P}hase
                      {S}eparation},
      journal      = {Molecular pharmaceutics},
      volume       = {18},
      number       = {11},
      issn         = {1543-8392},
      address      = {Washington, DC},
      publisher    = {American Chemical Society},
      reportid     = {FZJ-2021-03880},
      pages        = {4162–4169},
      year         = {2021},
      abstract     = {Antibody therapies are typically based on
                      high-concentration formulations that need to be administered
                      subcutaneously. These conditions induce several challenges,
                      inter alia a viscosity suitable for injection, sufficient
                      solution stability, and preservation of molecular function.
                      To obtain systematic insights into the molecular factors, we
                      study the dynamics on the molecular level under strongly
                      varying solution conditions. In particular, we use solutions
                      of antibodies with poly(ethylene glycol), in which simple
                      cooling from room temperature to freezing temperatures
                      induces a transition from a well-dispersed solution into a
                      phase-separated and macroscopically arrested system. Using
                      quasi-elastic neutron scattering during in situ cooling
                      ramps and in prethermalized measurements, we observe a
                      strong decrease in antibody diffusion, while internal
                      flexibility persists to a significant degree, thus ensuring
                      the movement necessary for the preservation of molecular
                      function. These results are relevant for a more dynamic
                      understanding of antibodies in high-concentration
                      formulations, which affects the formation of transient
                      clusters governing the solution viscosity.},
      cin          = {JCNS-4 / JCNS-1 / JCNS-FRM-II / MLZ},
      ddc          = {610},
      cid          = {I:(DE-Juel1)JCNS-4-20201012 / I:(DE-Juel1)JCNS-1-20110106 /
                      I:(DE-Juel1)JCNS-FRM-II-20110218 / I:(DE-588b)4597118-3},
      pnm          = {6G4 - Jülich Centre for Neutron Research (JCNS) (FZJ)
                      (POF4-6G4) / 632 - Materials – Quantum, Complex and
                      Functional Materials (POF4-632)},
      pid          = {G:(DE-HGF)POF4-6G4 / G:(DE-HGF)POF4-632},
      experiment   = {EXP:(DE-MLZ)KWS2-20140101 / EXP:(DE-MLZ)KWS3-20140101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:34637319},
      UT           = {WOS:000715212700020},
      doi          = {10.1021/acs.molpharmaceut.1c00555},
      url          = {https://juser.fz-juelich.de/record/901872},
}