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@ARTICLE{DaVela:830148,
      author       = {Da Vela, Stefano and Roosen-Runge, Felix and Skoda,
                      Maximilian W. A. and Jacobs, Robert M. J. and Seydel, Tilo
                      and Frielinghaus, Henrich and Sztucki, Michael and Schweins,
                      Ralf and Zhang, Fajun and Schreiber, Frank},
      title        = {{E}ffective {I}nteractions and {C}olloidal {S}tability of
                      {B}ovine γ-{G}lobulin in {S}olution},
      journal      = {The journal of physical chemistry / B},
      volume       = {121},
      number       = {23},
      issn         = {1089-5647},
      address      = {Washington, DC},
      publisher    = {Soc.},
      reportid     = {FZJ-2017-03725},
      pages        = {5759–5769},
      year         = {2017},
      abstract     = {Interactions and phase behavior of serum albumin and
                      γ-globulin are of fundamental interest in biophysical and
                      pharmaceutical research, as these are the most abundant
                      proteins in blood plasma. In this work, we report the
                      characterization of the oligomeric state of bovine
                      γ-globulin, the effective protein-protein interactions and
                      the colloidal stability in aqueous solution as a function of
                      protein concentration and ionic strength. Classical
                      biochemical techniques, such as size exclusion
                      chromatography (SEC) and gel electrophoresis together with
                      small angle X-ray and neutron scattering (SAXS/SANS) were
                      employed for this study. The results show that bovine
                      γ-globulin solutions are dominated by monomer and idiotype
                      anti-idiotype dimer. Despite the flexibility and highly
                      non-spherical shape of the protein, a simple model with a
                      disk-type form factor and a structure factor of a
                      square-well potential provide a valid description of the
                      scattering data. The overall interactions are attractive and
                      the strength decreases with increasing protein
                      concentration, or adding buffer or salts. For higher protein
                      volume fraction (> $7\%),$ the model leads to a strong
                      particle-particle correlation which does not appear in the
                      experimental data. This mismatch is most likely due to the
                      smearing effect of the conformation change of proteins in
                      solution. The stability of γ-globulin solutions is highly
                      sensitive to protein concentration, ionic strength and to
                      the type of added salts, such as NaCl, Na2SO4 and NaSCN. For
                      solutions below 50 mg/mL and at low ionic strengths (<
                      0.1M), protein aggregation is most likely due to
                      subpopulations of IgG molecules with attractive patches of
                      complementary surface charge. This effect is reduced for
                      higher protein concentration due to the self-buffering
                      effects. For high ionic strength (> 1M), typical salting-in
                      and salting-out effects are observed. Results are further
                      discussed in comparison with current studies in the
                      literature on monoclonal antibodies.},
      cin          = {JCNS (München) ; Jülich Centre for Neutron Science JCNS
                      (München) ; JCNS-FRM-II / Neutronenstreuung ; JCNS-1},
      ddc          = {530},
      cid          = {I:(DE-Juel1)JCNS-FRM-II-20110218 /
                      I:(DE-Juel1)JCNS-1-20110106},
      pnm          = {6G15 - FRM II / MLZ (POF3-6G15) / 6G4 - Jülich Centre for
                      Neutron Research (JCNS) (POF3-623)},
      pid          = {G:(DE-HGF)POF3-6G15 / G:(DE-HGF)POF3-6G4},
      experiment   = {EXP:(DE-MLZ)KWS2-20140101},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000403731400009},
      pubmed       = {pmid:28520443},
      doi          = {10.1021/acs.jpcb.7b03510},
      url          = {https://juser.fz-juelich.de/record/830148},
}