% IMPORTANT: The following is UTF-8 encoded.  This means that in the presence
% of non-ASCII characters, it will not work with BibTeX 0.99 or older.
% Instead, you should use an up-to-date BibTeX implementation like “bibtex8” or
% “biber”.

@ARTICLE{Schwaminger:859756,
      author       = {Schwaminger, Sebastian P. and Blank-Shim, Silvia A. and
                      Scheifele, Isabell and Pipich, Vitaliy and Fraga-García,
                      Paula and Berensmeier, Sonja},
      title        = {{D}esign of {I}nteractions {B}etween {N}anomaterials and
                      {P}roteins: {A} {H}ighly {A}ffine {P}eptide {T}ag to {B}are
                      {I}ron {O}xide {N}anoparticles for {M}agnetic {P}rotein
                      {S}eparation},
      journal      = {Biotechnology journal},
      volume       = {14},
      number       = {3},
      issn         = {1860-6768},
      address      = {Weinheim},
      publisher    = {Wiley-VCH},
      reportid     = {FZJ-2019-00593},
      pages        = {1800055 -},
      year         = {2019},
      abstract     = {Superparamagnetic nanoparticles have recently gained much
                      attention due to their broad range of applicability
                      including medical in vivo technologies, sensors and as
                      supports for catalysts. As magnetic affinity materials, they
                      can be utilized for the development of new purification
                      strategies for pharmaceuticals and other target molecules
                      from crude lysates. Here, a short peptide tag based on a
                      glutamate sequence is introduced and the adsorption of pure
                      protein as well as protein from crude cell lysate at
                      different conditions is demonstrated. Fused to a model
                      protein this tag can be used to recognize and purify this
                      protein from a fermentation broth by bare iron oxide
                      nanoparticles (BIONs). Binding of up to 0.2 g protein per g
                      nanoparticles can be achieved and recovered easily by
                      switching to a citrate buffered system. For a deeper
                      understanding of the separation process, the aggregation and
                      agglomeration of the nanoparticle protein systems were
                      monitored for binding and elution steps. Furthermore, an
                      upscaling of the process to the liter scale and the
                      separation of a green fluorescent protein (GFP) containing
                      the affinity tag to purities of $70\%$ from E. coli
                      fermentation broth was possible in a one step process by
                      means of high gradient magnetic separation (HGMS).},
      cin          = {JCNS-FRM-II / Neutronenstreuung ; JCNS-1},
      ddc          = {570},
      cid          = {I:(DE-Juel1)JCNS-FRM-II-20110218 /
                      I:(DE-Juel1)JCNS-1-20110106},
      pnm          = {6G4 - Jülich Centre for Neutron Research (JCNS) (POF3-623)
                      / 6G15 - FRM II / MLZ (POF3-6G15)},
      pid          = {G:(DE-HGF)POF3-6G4 / G:(DE-HGF)POF3-6G15},
      experiment   = {EXP:(DE-MLZ)KWS3-20140101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:29704407},
      UT           = {WOS:000460177400021},
      doi          = {10.1002/biot.201800055},
      url          = {https://juser.fz-juelich.de/record/859756},
}