The distribution and degradation of radiolabeled superparamagnetic iron oxide nanoparticles and quantum dots in mice

• Denise Bargheer,
• Artur Giemsa,
• Barbara Freund,
• Markus Heine,
• Christian Waurisch,
• Gordon M. Stachowski,
• Stephen G. Hickey,
• Alexander Eychmüller,
• Jörg Heeren and
• Peter Nielsen

Beilstein J. Nanotechnol. 2015, 6, 111–123, doi:10.3762/bjnano.6.11

• -demand” synthesis of 59Fe-SPIOs designed for in vivo experiments in animal models. It was coincidentally found that the SPIOs could similarly be tagged with 51CrCl3, likely due to the similarity between the Fe(III)- and Cr(III)-oxide chemistry. An attempted incorporation of the divalent cation 65ZnCl2 in

• accumulates in the liver. These results indicate a striking different metabolism of Cr3+ from these two sources. We know from previous experiments with the same SPIOs labeled with 59Fe instead of 51Cr that the iron oxide core of this particle is degraded to a large extent in the liver (data not shown). We

• elegantly used to study the absorption of intact nanoparticles from the gastrointestinal tract, an important topic in nanotoxicology. For this, 59Fe-labeled SPIOs were given by gavage to groups of mice and the 59Fe-WBR was followed in living mice for 14 d using a whole body counter (Figure 5A). Most of the

The fate of a designed protein corona on nanoparticles in vitro and in vivo

• Denise Bargheer,
• Julius Nielsen,
• Gabriella Gébel,
• Markus Heine,
• Sunhild C. Salmen,
• Roland Stauber,
• Horst Weller,
• Joerg Heeren and
• Peter Nielsen

Beilstein J. Nanotechnol. 2015, 6, 36–46, doi:10.3762/bjnano.6.5

• . These in vitro experiments show a clear difference in the stability of a preformed hard corona with adsorbed or covalently bound protein. This difference seems, however, to be of minor importance in vivo when polymer-coated 59Fe-SPIOs with adsorbed or covalently bound 125I-labeled mouse transferrin were

• injected intravenously in mice. With both protein coronae the 59Fe/125I-labelled particles were cleared from the blood stream within 30 min and appeared in the liver and spleen to a large extent (>90%). In addition, after 2 h already half of the 125I-labeled transferrin from both nanodevices was recycled

• vivo for the respective nanoparticle uptake. Keywords: albumin; 59Fe; 125I; organ uptake; protein corona; SPIOs; transferrin; Introduction Nanoparticles (NPs) have unique capabilities to interact with cells and organs which mark them as attractive working material in nanobioscience and nanomedicine

The cell-type specific uptake of polymer-coated or micelle-embedded QDs and SPIOs does not provoke an acute pro-inflammatory response in the liver

• Markus Heine,
• Alexander Bartelt,
• Oliver T. Bruns,
• Denise Bargheer,
• Artur Giemsa,
• Barbara Freund,
• Ludger Scheja,
• Christian Waurisch,
• Alexander Eychmüller,
• Rudolph Reimer,
• Horst Weller,
• Peter Nielsen and
• Joerg Heeren

Beilstein J. Nanotechnol. 2014, 5, 1432–1440, doi:10.3762/bjnano.5.155

• and 59Fe-SPIOs either by an amphiphilic polymer coat [21] or by the incorporation into the lipid core of micelles [17][18], as indicated in the schematic model (Figure 1A). The liver rapidly clears polymer-coated 59Fe-SPIOs [19], however the exact molecular mechanisms and cell types involved in the

• nanocrystals Encapsulation of nanocrystals was achieved as described [37] with slight modifications: 2 mL poly(maleic anhydride-alt-1-octadecene) (PMAOD) solution (concentration: 0.01 g/mL in CHCl3) were added to a solution of either 2 mg oleic acid stabilized SPIO, QDs or 59Fe-SPIOs [21] dissolved in 2 mL

• dissolved in chloroform and mixed with either SPIOs, QDs or with 59Fe-SPIOs [18][20]. After the solvent was evaporated, 1 mL of PBS was added and nanocrystals-containing lipid micelles were formed by sonication. Potential aggregates were removed by filtration using a 0.45 µm membranous filter prior to