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@ARTICLE{RussoKrauss:889062,
      author       = {Russo Krauss, Irene and Picariello, Alessandra and
                      Vitiello, Giuseppe and De Santis, Augusta and Koutsioumpas,
                      Alexandros and Houston, Judith E. and Fragneto, Giovanna and
                      Paduano, Luigi},
      title        = {{I}nteraction with {H}uman {S}erum {P}roteins {R}eveals
                      {B}iocompatibility of {P}hosphocholine-{F}unctionalized
                      {SPION}s and {F}ormation of {A}lbumin-{D}ecorated
                      {N}anoparticles},
      journal      = {Langmuir},
      volume       = {36},
      number       = {30},
      issn         = {1520-5827},
      address      = {Washington, DC},
      publisher    = {ACS Publ.},
      reportid     = {FZJ-2021-00005},
      pages        = {8777 - 8791},
      year         = {2020},
      abstract     = {Nanoparticles (NPs) are increasingly exploited as
                      diagnostic and therapeutic devices in medicine. Among them,
                      superparamagnetic nanoparticles (SPIONs) represent very
                      promising tools for magnetic resonance imaging, local
                      heaters for hyperthermia, and nanoplatforms for multimodal
                      imaging and theranostics. However, the use of NPs, including
                      SPIONs, in medicine presents several issues: first, the
                      encounter with the biological world and proteins in
                      particular. Indeed, nanoparticles can suffer from protein
                      adsorption, which can affect NP functionality and
                      biocompatibility. In this respect, we have investigated the
                      interaction of small SPIONs covered by an amphiphilic double
                      layer of oleic acid/oleylamine and
                      1-octadecanoyl-sn-glycero-3-phosphocholine with two abundant
                      human plasma proteins, human serum albumin (HSA) and human
                      transferrin. By means of spectroscopic and scattering
                      techniques, we analyzed the effect of SPIONs on protein
                      structure and the binding affinities, and only found strong
                      binding in the case of HSA. In no case did SPIONs alter the
                      protein structure significantly. We structurally
                      characterized HSA/SPIONs complexes by means of light and
                      neutron scattering, highlighting the formation of a
                      monolayer of protein molecules on the NP surface. Their
                      interaction with lipid bilayers mimicking biological
                      membranes was investigated by means of neutron reflectivity.
                      We show that HSA/SPIONs do not affect lipid bilayer features
                      and could be further exploited as a nanoplatform for future
                      applications. Overall, our findings point toward a high
                      biocompatibility of phosphocholine-decorated SPIONs and
                      support their use in nanomedicine.},
      cin          = {JCNS-FRM-II / JCNS-1 / MLZ / JCNS-4},
      ddc          = {540},
      cid          = {I:(DE-Juel1)JCNS-FRM-II-20110218 /
                      I:(DE-Juel1)JCNS-1-20110106 / I:(DE-588b)4597118-3 /
                      I:(DE-Juel1)JCNS-4-20201012},
      pnm          = {6215 - Soft Matter, Health and Life Sciences (POF3-621) /
                      6G4 - Jülich Centre for Neutron Research (JCNS) (POF3-623)
                      / 6G15 - FRM II / MLZ (POF3-6G15)},
      pid          = {G:(DE-HGF)POF3-6215 / G:(DE-HGF)POF3-6G4 /
                      G:(DE-HGF)POF3-6G15},
      experiment   = {EXP:(DE-MLZ)MARIA-20140101 / EXP:(DE-MLZ)KWS2-20140101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {32575987},
      UT           = {WOS:000558755200013},
      doi          = {10.1021/acs.langmuir.0c01083},
      url          = {https://juser.fz-juelich.de/record/889062},
}