Cargando…

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 (125)I-labeled test proteins (transferrin, albumin), the binding and exchange of corona proteins wa...

Descripción completa

Detalles Bibliográficos
Autores principales: Bargheer, Denise, Nielsen, Julius, Gébel, Gabriella, Heine, Markus, Salmen, Sunhild C, Stauber, Roland, Weller, Horst, Heeren, Joerg, Nielsen, Peter
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Beilstein-Institut 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4311732/
https://www.ncbi.nlm.nih.gov/pubmed/25671150
http://dx.doi.org/10.3762/bjnano.6.5
_version_ 1782355048620097536
author Bargheer, Denise
Nielsen, Julius
Gébel, Gabriella
Heine, Markus
Salmen, Sunhild C
Stauber, Roland
Weller, Horst
Heeren, Joerg
Nielsen, Peter
author_facet Bargheer, Denise
Nielsen, Julius
Gébel, Gabriella
Heine, Markus
Salmen, Sunhild C
Stauber, Roland
Weller, Horst
Heeren, Joerg
Nielsen, Peter
author_sort Bargheer, Denise
collection PubMed
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 (125)I-labeled test proteins (transferrin, albumin), the binding and exchange of corona proteins was studied first in vitro. Incubation with (125)I-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 (125)I-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 (59)Fe-SPIOs with adsorbed or covalently bound (125)I-labeled mouse transferrin were injected intravenously in mice. With both protein coronae the (59)Fe/(125)I-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 (125)I-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.
format Online
Article
Text
id pubmed-4311732
institution National Center for Biotechnology Information
language English
publishDate 2015
publisher Beilstein-Institut
record_format MEDLINE/PubMed
spelling pubmed-43117322015-02-10 The fate of a designed protein corona on nanoparticles in vitro and in vivo Bargheer, Denise Nielsen, Julius Gébel, Gabriella Heine, Markus Salmen, Sunhild C Stauber, Roland Weller, Horst Heeren, Joerg Nielsen, Peter Beilstein J Nanotechnol Full Research Paper 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 (125)I-labeled test proteins (transferrin, albumin), the binding and exchange of corona proteins was studied first in vitro. Incubation with (125)I-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 (125)I-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 (59)Fe-SPIOs with adsorbed or covalently bound (125)I-labeled mouse transferrin were injected intravenously in mice. With both protein coronae the (59)Fe/(125)I-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 (125)I-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. Beilstein-Institut 2015-01-06 /pmc/articles/PMC4311732/ /pubmed/25671150 http://dx.doi.org/10.3762/bjnano.6.5 Text en Copyright © 2015, Bargheer et al. https://creativecommons.org/licenses/by/2.0https://www.beilstein-journals.org/bjnano/termsThis is an Open Access article under the terms of the Creative Commons Attribution License (https://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. The license is subject to the Beilstein Journal of Nanotechnology terms and conditions: (https://www.beilstein-journals.org/bjnano/terms)
spellingShingle Full Research Paper
Bargheer, Denise
Nielsen, Julius
Gébel, Gabriella
Heine, Markus
Salmen, Sunhild C
Stauber, Roland
Weller, Horst
Heeren, Joerg
Nielsen, Peter
The fate of a designed protein corona on nanoparticles in vitro and in vivo
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 Full Research Paper
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4311732/
https://www.ncbi.nlm.nih.gov/pubmed/25671150
http://dx.doi.org/10.3762/bjnano.6.5
work_keys_str_mv AT bargheerdenise thefateofadesignedproteincoronaonnanoparticlesinvitroandinvivo
AT nielsenjulius thefateofadesignedproteincoronaonnanoparticlesinvitroandinvivo
AT gebelgabriella thefateofadesignedproteincoronaonnanoparticlesinvitroandinvivo
AT heinemarkus thefateofadesignedproteincoronaonnanoparticlesinvitroandinvivo
AT salmensunhildc thefateofadesignedproteincoronaonnanoparticlesinvitroandinvivo
AT stauberroland thefateofadesignedproteincoronaonnanoparticlesinvitroandinvivo
AT wellerhorst thefateofadesignedproteincoronaonnanoparticlesinvitroandinvivo
AT heerenjoerg thefateofadesignedproteincoronaonnanoparticlesinvitroandinvivo
AT nielsenpeter thefateofadesignedproteincoronaonnanoparticlesinvitroandinvivo
AT bargheerdenise fateofadesignedproteincoronaonnanoparticlesinvitroandinvivo
AT nielsenjulius fateofadesignedproteincoronaonnanoparticlesinvitroandinvivo
AT gebelgabriella fateofadesignedproteincoronaonnanoparticlesinvitroandinvivo
AT heinemarkus fateofadesignedproteincoronaonnanoparticlesinvitroandinvivo
AT salmensunhildc fateofadesignedproteincoronaonnanoparticlesinvitroandinvivo
AT stauberroland fateofadesignedproteincoronaonnanoparticlesinvitroandinvivo
AT wellerhorst fateofadesignedproteincoronaonnanoparticlesinvitroandinvivo
AT heerenjoerg fateofadesignedproteincoronaonnanoparticlesinvitroandinvivo
AT nielsenpeter fateofadesignedproteincoronaonnanoparticlesinvitroandinvivo