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@ARTICLE{Ramm:903752,
      author       = {Ramm, Ingrid and Sanchez-Fernandez, Adrian and Choi,
                      Jaeyeong and Lang, Christian and Schagerlöf, Herje and
                      Wahlgren, Marie and Nilsson, Lars},
      title        = {{T}he {I}mpact of {G}lycerol on an {A}ffibody
                      {C}onformation and {I}ts {C}orrelation to {C}hemical
                      {D}egradation},
      journal      = {Pharmaceutics},
      volume       = {13},
      number       = {11},
      issn         = {1999-4923},
      address      = {Basel},
      publisher    = {MDPI},
      reportid     = {FZJ-2021-05392},
      pages        = {1853 -},
      year         = {2021},
      abstract     = {The addition of glycerol to protein solutions is often used
                      to hinder the aggregation and denaturation of proteins.
                      However, it is not a generalised practice against chemical
                      degradation reactions. The chemical degradation of proteins,
                      such as deamidation and isomerisation, is an important
                      deteriorative mechanism that leads to a loss of
                      functionality of pharmaceutical proteins. Here, the
                      influence of glycerol on the chemical degradation of a
                      protein and its correlation to glycerol-induced
                      conformational changes is presented. The time-dependent
                      chemical degradation of a pharmaceutical protein, GA-Z, in
                      the absence and presence of glycerol was investigated in a
                      stability study. The effect of glycerol on protein
                      conformation and oligomerisation was characterised using
                      asymmetric field-flow fractionation and small-angle neutron
                      scattering in a wide glycerol concentration range of
                      $0–90\%$ v/v. The results from the stability study were
                      connected to the observed glycerol-induced conformational
                      changes in the protein. A correlation between protein
                      conformation and the protective effect of glycerol against
                      the degradation reactions deamidation, isomerisation, and
                      hydrolysis was found. The study reveals that glycerol
                      induces conformational changes of the protein, which favour
                      a more compact and chemically stable state. It is also shown
                      that the conformation can be changed by other system
                      properties, e.g., protein concentration, leading to
                      increased chemical stability.},
      cin          = {JCNS-FRM-II / JCNS-1 / JCNS-4 / MLZ},
      ddc          = {610},
      cid          = {I:(DE-Juel1)JCNS-FRM-II-20110218 /
                      I:(DE-Juel1)JCNS-1-20110106 / I:(DE-Juel1)JCNS-4-20201012 /
                      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},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {34834267},
      UT           = {WOS:000792960900014},
      doi          = {10.3390/pharmaceutics13111853},
      url          = {https://juser.fz-juelich.de/record/903752},
}