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@ARTICLE{LeCur:203311,
      author       = {Le Cœur, Clémence and Combet, Sophie and Carrot,
                      Géraldine and Busch, Peter and Teixeira, José and
                      Longeville, Stéphane},
      title        = {{C}onformation of the {P}oly(ethylene {G}lycol) {C}hains in
                      {D}i{PEG}ylated {H}emoglobin {S}pecifically {P}robed by
                      {SANS}: {C}orrelation with {PEG} {L}ength and in {V}ivo
                      {E}fficiency},
      journal      = {Langmuir},
      volume       = {31},
      number       = {30},
      issn         = {1520-5827},
      address      = {Washington, DC},
      publisher    = {ACS Publ.},
      reportid     = {FZJ-2015-05278},
      pages        = {8402 - 8410},
      year         = {2015},
      abstract     = {Cell-free hemoglobin (Hb)-based oxygen carriers have long
                      been proposed as blood substitutes but their clinical use
                      remains tricky due to problems of inefficiency and/or
                      toxicity. Conjugation of Hb with the biocompatible polymer
                      poly(ethylene glycol) (PEG) greatly improved their
                      performance. However, physiological data suggested a polymer
                      molecular weight (Mw) threshold of about 10 kDa, beyond
                      which the grafting of two PEG chains no longer improves
                      efficiency and nontoxicity of diPEG/Hb conjugates. We used
                      small-angle neutron scattering and contrast variation, which
                      are the only techniques able to probe separately the
                      conformation of PEG chains and Hb protein within the
                      complex, to investigate the role of PEG chain conformation
                      in diPEGylated Hb conjugates as a function of the polymer
                      Mw. We found out that the structure of Hb tetramer is not
                      modified by the polymer grafting. Similarly, with a constant
                      grafting of two chains per protein, there is no significant
                      change of the Gaussian conformation between free and grafted
                      PEG below ∼10 kDa, the complex being well described by the
                      “dumbbell” model. However, beyond that threshold, the
                      radius of gyration of grafted PEG is significantly smaller
                      than that of the free polymer, showing a compaction of the
                      PEG chains, either in the “dumbbell” model or in the
                      “shroud” one. In the latter model, the polymer may be
                      wrapped on the surface of the protein spreading a protective
                      “shielding” effect over a larger fraction of the
                      protein. Both proposed models are in good agreement with the
                      physiological data reported in the literature.},
      cin          = {JCNS (München) ; Jülich Centre for Neutron Science JCNS
                      (München) ; JCNS-FRM-II / Neutronenstreuung ; JCNS-1},
      ddc          = {670},
      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:000359278000025},
      doi          = {10.1021/acs.langmuir.5b01121},
      url          = {https://juser.fz-juelich.de/record/203311},
}