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@INBOOK{SchmittKopplin:821058,
      author       = {Pattky, Martin and Barkovits, Katalin and Marcus, Katrin
                      and Weiergräber, Oliver H. and Huhn, Carolin},
      editor       = {Schmitt-Kopplin, Philippe},
      title        = {{S}tatically {A}dsorbed {C}oatings for {H}igh {S}eparation
                      {E}fficiency and {R}esolution in {CE}–{MS} {P}eptide
                      {A}nalysis: {S}trategies and {I}mplementation},
      volume       = {1483},
      address      = {New York, NY},
      publisher    = {Springer New York},
      reportid     = {FZJ-2016-06302},
      isbn         = {978-1-4939-6401-7 (print)},
      series       = {Methods in Molecular Biology},
      pages        = {53 - 75},
      year         = {2016},
      comment      = {Capillary Electrophoresis / Schmitt-Kopplin, Philippe
                      (Editor) ; New York, NY : Springer New York, 2016, Chapter 4
                      ; ISSN: 1064-3745=1940-6029 ; ISBN:
                      978-1-4939-6401-7=978-1-4939-6403-1 ;
                      doi:10.1007/978-1-4939-6403-1},
      booktitle     = {Capillary Electrophoresis /
                       Schmitt-Kopplin, Philippe (Editor) ;
                       New York, NY : Springer New York, 2016,
                       Chapter 4 ; ISSN: 1064-3745=1940-6029 ;
                       ISBN:
                       978-1-4939-6401-7=978-1-4939-6403-1 ;
                       doi:10.1007/978-1-4939-6403-1},
      abstract     = {Coatings are necessary to prevent protein and peptide
                      adsorption to the capillary surface and obtain high
                      intermediate precision. In this protocol, we first present
                      our basic strategy to address peptide separation using three
                      different coatings: one neutral and two cationic coatings,
                      the latter largely differing in their induced electroosmotic
                      mobility. In detail, we will describe how we apply the
                      statically adsorbed coatings to obtain very high plate
                      numbers and high repeatability.With some model examples, we
                      clearly describe the scope of the method for the analysis of
                      peptide samples: tryptic digests are addressed as well as
                      small glycoproteins and glycopeptides largely differing in
                      their effective electrophoretic mobility. We also show that
                      the method is suitable for a fast screening of peptide
                      samples despite a high matrix load comprising of up to 500
                      mmol/L sodium chloride. We demonstrate that this basic CE-MS
                      method is rather independent of the polarity of the analytes
                      with a very fast near-baseline separation of very
                      hydrophobic Aβ peptides related to the onset of Alzheimer's
                      disease. These examples will give an impression, which
                      coating is most suitable for a specific analytical
                      application.Special attention is paid to difficult aspects
                      of the coating procedure and the CE-MS method, e.g., the
                      potential of cross-contamination when changing the
                      coatings.},
      cin          = {ICS-6},
      ddc          = {570},
      cid          = {I:(DE-Juel1)ICS-6-20110106},
      pnm          = {552 - Engineering Cell Function (POF3-552)},
      pid          = {G:(DE-HGF)POF3-552},
      typ          = {PUB:(DE-HGF)7},
      UT           = {WOS:000398304300005},
      doi          = {10.1007/978-1-4939-6403-1_4},
      url          = {https://juser.fz-juelich.de/record/821058},
}