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@ARTICLE{Papagiannopoulos:845244,
      author       = {Papagiannopoulos, Aristeidis and Karayianni, Maria and
                      Pispas, Stergios and Radulescu, Aurel},
      title        = {{F}ormation of complexes in aqueous solutions of
                      amphiphilic triblock polyelectrolytes of different
                      topologies and an oppositely charged protein},
      journal      = {Soft matter},
      volume       = {14},
      number       = {15},
      issn         = {1744-6848},
      address      = {London},
      publisher    = {Royal Soc. of Chemistry},
      reportid     = {FZJ-2018-02527},
      pages        = {2860 - 2869},
      year         = {2018},
      abstract     = {The complexation of lysozyme with aggregates from two
                      triblock amphiphilic polyelectrolytes of the same blocks but
                      different topologies and block molar masses, namely
                      PS-b-SCPI-b-PEO and SCPI-b-PS-b-PEO, is investigated by
                      scattering and spectroscopy methods. Light scattering
                      reveals that the interaction with lysozyme causes shrinkage
                      of the self-assembled nanoparticles in the case of the
                      hydrophobic–polyelectrolyte–hydrophilic sequence. In the
                      polyelectrolyte–hydrophobic–hydrophilic sequence, the
                      opposite trend is observed. Small angle neutron scattering
                      confirms the existence of micellar and fractal aggregates
                      and the complexation with lysozyme. The pH-dependence of the
                      interactions and the stability of the hybrid protein/polymer
                      nanoparticles upon salt addition are tested. The native
                      conformation of the protein is found to be preserved during
                      complexation. This study reveals that both micellar and
                      fractal aggregates made of amphiphilic triblock
                      polyelectrolytes are capable of loading with oppositely
                      charged proteins in a controllable manner, tuned primarily
                      by the structure of the triblock terpolymer.},
      cin          = {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},
      pubmed       = {pmid:29565433},
      UT           = {WOS:000435995900013},
      doi          = {10.1039/C8SM00208H},
      url          = {https://juser.fz-juelich.de/record/845244},
}