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@ARTICLE{Bhler:587024,
      author       = {Böhler, Hendrik and Orth-Alampour, Setareh and Baaten,
                      Constance and Riedner, Maria and Jankowski, Joachim and
                      Beck, Tobias},
      title        = {{A}ssembly of chemically modified protein nanocages into
                      3{D} materials for the adsorption of uremic toxins},
      journal      = {Journal of materials chemistry / B},
      volume       = {11},
      number       = {1},
      issn         = {2050-750X},
      address      = {London ˜[u.a.]œ},
      publisher    = {RSC},
      reportid     = {PUBDB-2023-04092},
      pages        = {55 - 60},
      year         = {2022},
      abstract     = {Hemodialysis fails to remove protein-bound uremic toxins
                      that are attributed with high cardiovascular risk.
                      Application of adsorption materials is a viable strategy,
                      but suitable biocompatible adsorbents are still not
                      available. Here, we demonstrate that adsorbents based on the
                      bottom-up assembly of the intrinsically biocompatible
                      protein cage ferritin are applicable for toxin adsorption.
                      Due to the size-exclusion effect of its pores, only small
                      molecules such as uremic toxins can enter the protein cage.
                      Protein redesign techniques that target selectively the
                      inner surface were used to introduce anchor sites for
                      chemical modification. Porous crystalline adsorbents were
                      fabricated by bottom-up assembly of the protein cage.
                      Linkage of up to 96 phenylic or aliphatic molecules per
                      container was verified by ESI-MS. Materials based on
                      unmodified ferritin cages can already adsorb the uremic
                      toxins. The adsorption capacity could be increased by about
                      $50\%$ through functionalization with hydrophobic molecules
                      reaching 458 μg g$^{−1}$ for indoxyl sulfate. The
                      biohybrid materials show no contamination with endotoxins
                      and do not activate blood platelets. These findings
                      demonstrate the great potential of protein-based adsorbents
                      for the clearance of uremic toxins: modifications enhance
                      toxin adsorption without diminishing the biocompatibility of
                      the final protein-based material.},
      cin          = {DOOR ; HAS-User},
      ddc          = {610},
      cid          = {I:(DE-H253)HAS-User-20120731},
      pnm          = {6G3 - PETRA III (DESY) (POF4-6G3) / FS-Proposal: I-20211171
                      (I-20211171) / FS-Proposal: I-20210277 (I-20210277) / DFG
                      project 401323995 - Hochstrukturierte optische Materialien
                      aus Proteincontainern und plasmonischen Nanopartikeln für
                      die Manipulation von Licht auf der Nanoskala (401323995) /
                      DFG project 390715994 - EXC 2056: CUI: Advanced Imaging of
                      Matter (390715994) / DFG project 413227073 -
                      UPLC-ESI-QTRAP-Massenspektrometer (413227073) / GRK 2536 -
                      GRK 2536: Hybridstrukturen auf der Nanometerskala: Chemische
                      Konzepte zur Herstellung heterogener Nanostrukturen mit
                      anisotropen Materialeigenschaften (NANOHYBRID) (408076438)},
      pid          = {G:(DE-HGF)POF4-6G3 / G:(DE-H253)I-20211171 /
                      G:(DE-H253)I-20210277 / G:(GEPRIS)401323995 /
                      G:(GEPRIS)390715994 / G:(GEPRIS)413227073 /
                      G:(GEPRIS)408076438},
      experiment   = {EXP:(DE-H253)P-P11-20150101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:36504125},
      UT           = {WOS:000897611200001},
      doi          = {10.1039/D2TB02386E},
      url          = {https://bib-pubdb1.desy.de/record/587024},
}