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@ARTICLE{Siefker:856725,
      author       = {Siefker, Justin and Biehl, Ralf and Kruteva, Margarita and
                      Feoktystov, Artem and Coppens, Marc-Olivier},
      title        = {{C}onfinement {F}acilitated {P}rotein {S}tabilization {A}s
                      {I}nvestigated by {S}mall-{A}ngle {N}eutron {S}cattering},
      journal      = {Journal of the American Chemical Society},
      volume       = {140},
      number       = {40},
      issn         = {1520-5126},
      address      = {Washington, DC},
      publisher    = {American Chemical Society},
      reportid     = {FZJ-2018-06076},
      pages        = {12720 - 12723},
      year         = {2018},
      abstract     = {While mesoporous silicas have been shown to bea compelling
                      candidate for drug delivery and the implemen-tation of
                      biotechnological applications requiring protein
                      con-finement and immobilization, the understanding of
                      protein be-haviour upon physical adsorption into silica
                      pores is limited.Many indirect methods are available to
                      assess general adsorbedproteinstability,
                      suchasFTIRandactivityassays. However, thelimitation of these
                      methods is that spatial protein arrangementwithin the pores
                      cannot be assessed. Mesoporous silicas pose adistinct
                      challenge to direct methods, such as TEM, which lacksthe
                      contrast and resolution required to adequately observe
                      im-mobilized protein structure, and NMR, which is
                      computation-ally intensive and requires knowledge of the
                      primary structurea priori. Small-angle neutron scattering
                      (SANS) can surmountthese limitations and observe spatial
                      protein arrangement withinpores. Hereby, we observe the
                      stabilization of fluid-like proteinarrangement, facilitated
                      by geometry-dependent crowding ef-fects in cylindrical pores
                      of ordered mesoporous silica, SBA-15.Stabilization is
                      induced from a fluid-like structure factor, whichis
                      observed for samples at maximum protein loading in
                      SBA-15with pore diameters of 6.4 and 8.1 nm. Application of
                      thiseffect for prevention of irreversible aggregation in
                      high concen-tration environments is proposed.},
      cin          = {JCNS-FRM-II / Neutronenstreuung ; JCNS-1},
      ddc          = {540},
      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)KWS1-20140101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:30260637},
      UT           = {WOS:000447354800014},
      doi          = {10.1021/jacs.8b08454},
      url          = {https://juser.fz-juelich.de/record/856725},
}