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@ARTICLE{Papagiannopoulos:824287,
      author       = {Papagiannopoulos, Aristeidis and Meristoudi, Anastasia and
                      Pispas, Stergios and Radulescu, Aurel},
      title        = {{M}icelles from {HOOC}-{P}n{BA}- b -{PAA}-{C}$_{12}$
                      {H}$_{15}$ {D}iblock {A}mphiphilic {P}olyelectrolytes as
                      {P}rotein {N}anocarriers},
      journal      = {Biomacromolecules},
      volume       = {17},
      number       = {11},
      issn         = {1526-4602},
      address      = {Columbus, Ohio},
      publisher    = {American Chemical Soc.},
      reportid     = {FZJ-2016-06906},
      pages        = {3816 - 3827},
      year         = {2016},
      abstract     = {We investigate the potential of self-assembled
                      nanostructures of the PnBA-b-PAA amphiphilic diblock
                      polyelectrolyte as candidates for protein nanocarriers.
                      Three PnBA-b-PAA copolymers with different molecular weights
                      and PnBA/PAA weight ratios are tested. The system with the
                      most well-defined core–shell micellar structure is chosen
                      for complexation with lysozyme. Its solutions are found to
                      contain well-defined core–shell micelles that are stable
                      upon increase in solution salt content to physiological
                      levels. Upon mixing with lysozyme we find that the protein
                      globules accumulate preferably at the outer parts of the
                      hydrated corona of the micelles. Increasing the protein
                      concentration, intermicellar aggregation is enhanced in a
                      controllable way. At high salt content the number of
                      proteins per micelle is lower compared with the low salt
                      content, which points to an interaction of predominantly
                      electrostatic nature. While light scattering is very
                      sensitive to complexation, small-angle neutron scattering is
                      able to distinguish between the contributions from
                      individual micelles and aggregates. This work demonstrates
                      the use of scattering techniques to characterize
                      protein–polymer interactions in multiple hierarchical
                      levels.},
      cin          = {JCNS (München) ; Jülich Centre for Neutron Science JCNS
                      (München) ; JCNS-FRM-II / Neutronenstreuung ; JCNS-1 /
                      ICS-1},
      ddc          = {540},
      cid          = {I:(DE-Juel1)JCNS-FRM-II-20110218 /
                      I:(DE-Juel1)JCNS-1-20110106 / I:(DE-Juel1)ICS-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)KWS1-20140101},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000388155400038},
      doi          = {10.1021/acs.biomac.6b01408},
      url          = {https://juser.fz-juelich.de/record/824287},
}