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@ARTICLE{Chu:136114,
      author       = {Chu, Nam Ky and Olschewski, Diana and Seidel, Ralf and
                      Winklhofer, Konstanze F and Tatzelt, Jörg and Engelhard,
                      Martin and Becker, Christian F W},
      title        = {{P}rotein immobilization on liposomes and lipid-coated
                      nanoparticles by protein trans-splicing.},
      journal      = {Journal of peptide science},
      volume       = {16},
      number       = {10},
      issn         = {1075-2617},
      address      = {New York, NY [u.a.]},
      publisher    = {Wiley},
      reportid     = {DZNE-2020-02436},
      pages        = {582-588},
      year         = {2010},
      abstract     = {A plethora of methods exist to link proteins to surfaces in
                      order to generate functionalized materials. However, general
                      tools that lead to functional immobilization of
                      recombinantly expressed proteins on membranes such as
                      liposomes or lipid-coated nanoparticles are rare. Here we
                      present an approach that takes advantage of a
                      double-palmitoylated peptide that mediates stable membrane
                      anchoring in combination with protein trans-splicing for
                      efficient immobilization of recombinant proteins fused to
                      split intein segments. Two different DnaE split inteins from
                      Synechocystis and Nostoc punctiforme are tested and compared
                      to immobilization via direct native chemical ligation using
                      a protein thioester. Protein trans-splicing proceeds at low
                      protein concentrations and leads to functionalized vesicles
                      and membrane-coated silica nanoparticles.},
      keywords     = {Immobilized Proteins: chemistry / Immobilized Proteins:
                      metabolism / Inteins: genetics / Lipids: chemistry /
                      Liposomes: metabolism / Models, Molecular / Nanoparticles:
                      chemistry / Nostoc: genetics / Protein Splicing /
                      Recombinant Fusion Proteins: chemistry / Recombinant Fusion
                      Proteins: genetics / Recombinant Fusion Proteins: metabolism
                      / Synechocystis: genetics / Trans-Splicing / Immobilized
                      Proteins (NLM Chemicals) / Lipids (NLM Chemicals) /
                      Liposomes (NLM Chemicals) / Recombinant Fusion Proteins (NLM
                      Chemicals)},
      cin          = {München common},
      ddc          = {540},
      cid          = {I:(DE-2719)6000016},
      pnm          = {341 - Molecular Signaling (POF3-341) / 342 - Disease
                      Mechanisms and Model Systems (POF3-342)},
      pid          = {G:(DE-HGF)POF3-341 / G:(DE-HGF)POF3-342},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:20862726},
      doi          = {10.1002/psc.1227},
      url          = {https://pub.dzne.de/record/136114},
}