The fate of a designed protein corona on nanoparticles in vitro and in vivo
A variety of monodisperse superparamagnetic iron oxide particles (SPIOs) was designed in which the surface was modified by PEGylation with mono- or bifunctional poly(ethylene oxide)amines (PEG). Using 125I-labeled test proteins (transferrin, albumin), the binding and exchange of corona proteins was...
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| Format: | Article |
| Language: | English |
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Beilstein-Institut
2015-01-01
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| Series: | Beilstein Journal of Nanotechnology |
| Subjects: | |
| Online Access: | https://doi.org/10.3762/bjnano.6.5 |
| _version_ | 1811228342287859712 |
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| author | Denise Bargheer Julius Nielsen Gabriella Gébel Markus Heine Sunhild C. Salmen Roland Stauber Horst Weller Joerg Heeren Peter Nielsen |
| author_facet | Denise Bargheer Julius Nielsen Gabriella Gébel Markus Heine Sunhild C. Salmen Roland Stauber Horst Weller Joerg Heeren Peter Nielsen |
| author_sort | Denise Bargheer |
| collection | DOAJ |
| description | A variety of monodisperse superparamagnetic iron oxide particles (SPIOs) was designed in which the surface was modified by PEGylation with mono- or bifunctional poly(ethylene oxide)amines (PEG). Using 125I-labeled test proteins (transferrin, albumin), the binding and exchange of corona proteins was studied first in vitro. Incubation with 125I-transferrin showed that with increasing grade of PEGylation the binding was substantially diminished without a difference between simply adsorbed and covalently bound protein. However, after incubation with excess albumin and subsequently whole plasma, transferrin from the preformed transferrin corona was more and more lost from SPIOs in the case of adsorbed proteins. If non-labeled transferrin was used as preformed corona and excess 125I-labeled albumin was added to the reaction mixtures with different SPIOs, a substantial amount of label was bound to the particles with initially adsorbed transferrin but little or even zero with covalently bound transferrin. 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 back into the plasma and into tissue. This study confirms that adsorbed transferrin from a preformed protein corona is efficiently taken up by cells. It is also highlighted that a radiolabelling technique described in this study may be of value to investigate the role of protein corona formation in vivo for the respective nanoparticle uptake. |
| first_indexed | 2024-04-12T09:57:25Z |
| format | Article |
| id | doaj.art-5e249edb930e4dde940e411956287486 |
| institution | Directory Open Access Journal |
| issn | 2190-4286 |
| language | English |
| last_indexed | 2024-04-12T09:57:25Z |
| publishDate | 2015-01-01 |
| publisher | Beilstein-Institut |
| record_format | Article |
| series | Beilstein Journal of Nanotechnology |
| spelling | doaj.art-5e249edb930e4dde940e4119562874862022-12-22T03:37:39ZengBeilstein-InstitutBeilstein Journal of Nanotechnology2190-42862015-01-0161364610.3762/bjnano.6.52190-4286-6-5The fate of a designed protein corona on nanoparticles in vitro and in vivoDenise Bargheer0Julius Nielsen1Gabriella Gébel2Markus Heine3Sunhild C. Salmen4Roland Stauber5Horst Weller6Joerg Heeren7Peter Nielsen8Department of Biochemistry and Molecular Cell Biology, University Medical Center Hamburg-Eppendorf, Martinistr. 52, 20246 Hamburg, GermanyDepartment of Biochemistry and Molecular Cell Biology, University Medical Center Hamburg-Eppendorf, Martinistr. 52, 20246 Hamburg, GermanyDepartment of Biochemistry and Molecular Cell Biology, University Medical Center Hamburg-Eppendorf, Martinistr. 52, 20246 Hamburg, GermanyDepartment of Biochemistry and Molecular Cell Biology, University Medical Center Hamburg-Eppendorf, Martinistr. 52, 20246 Hamburg, GermanyInstitute of Physical Chemistry, University Hamburg, Grindelallee 117, 20146 Hamburg, GermanyMolecular and Cellular Oncology, ENT/University Medical Center Mainz, Langenbeckstr. 1, 55101 Mainz, GermanyInstitute of Physical Chemistry, University Hamburg, Grindelallee 117, 20146 Hamburg, GermanyDepartment of Biochemistry and Molecular Cell Biology, University Medical Center Hamburg-Eppendorf, Martinistr. 52, 20246 Hamburg, GermanyDepartment of Biochemistry and Molecular Cell Biology, University Medical Center Hamburg-Eppendorf, Martinistr. 52, 20246 Hamburg, GermanyA variety of monodisperse superparamagnetic iron oxide particles (SPIOs) was designed in which the surface was modified by PEGylation with mono- or bifunctional poly(ethylene oxide)amines (PEG). Using 125I-labeled test proteins (transferrin, albumin), the binding and exchange of corona proteins was studied first in vitro. Incubation with 125I-transferrin showed that with increasing grade of PEGylation the binding was substantially diminished without a difference between simply adsorbed and covalently bound protein. However, after incubation with excess albumin and subsequently whole plasma, transferrin from the preformed transferrin corona was more and more lost from SPIOs in the case of adsorbed proteins. If non-labeled transferrin was used as preformed corona and excess 125I-labeled albumin was added to the reaction mixtures with different SPIOs, a substantial amount of label was bound to the particles with initially adsorbed transferrin but little or even zero with covalently bound transferrin. 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 back into the plasma and into tissue. This study confirms that adsorbed transferrin from a preformed protein corona is efficiently taken up by cells. It is also highlighted that a radiolabelling technique described in this study may be of value to investigate the role of protein corona formation in vivo for the respective nanoparticle uptake.https://doi.org/10.3762/bjnano.6.5albumin59Fe125Iorgan uptakeprotein coronaSPIOstransferrin |
| spellingShingle | Denise Bargheer Julius Nielsen Gabriella Gébel Markus Heine Sunhild C. Salmen Roland Stauber Horst Weller Joerg Heeren Peter Nielsen The fate of a designed protein corona on nanoparticles in vitro and in vivo Beilstein Journal of Nanotechnology albumin 59Fe 125I organ uptake protein corona SPIOs transferrin |
| title | The fate of a designed protein corona on nanoparticles in vitro and in vivo |
| title_full | The fate of a designed protein corona on nanoparticles in vitro and in vivo |
| title_fullStr | The fate of a designed protein corona on nanoparticles in vitro and in vivo |
| title_full_unstemmed | The fate of a designed protein corona on nanoparticles in vitro and in vivo |
| title_short | The fate of a designed protein corona on nanoparticles in vitro and in vivo |
| title_sort | fate of a designed protein corona on nanoparticles in vitro and in vivo |
| topic | albumin 59Fe 125I organ uptake protein corona SPIOs transferrin |
| url | https://doi.org/10.3762/bjnano.6.5 |
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