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Interaction with Human Serum Proteins Reveals Biocompatibility of Phosphocholine-Functionalized SPIONs and Formation of Albumin-Decorated Nanoparticles

[Image: see text] 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 ima...

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Autores principales: Russo Krauss, Irene, Picariello, Alessandra, Vitiello, Giuseppe, De Santis, Augusta, Koutsioubas, Alexandros, Houston, Judith E., Fragneto, Giovanna, Paduano, Luigi
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Chemical Society 2020
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8008447/
https://www.ncbi.nlm.nih.gov/pubmed/32575987
http://dx.doi.org/10.1021/acs.langmuir.0c01083
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author Russo Krauss, Irene
Picariello, Alessandra
Vitiello, Giuseppe
De Santis, Augusta
Koutsioubas, Alexandros
Houston, Judith E.
Fragneto, Giovanna
Paduano, Luigi
author_facet Russo Krauss, Irene
Picariello, Alessandra
Vitiello, Giuseppe
De Santis, Augusta
Koutsioubas, Alexandros
Houston, Judith E.
Fragneto, Giovanna
Paduano, Luigi
author_sort Russo Krauss, Irene
collection PubMed
description [Image: see text] 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.
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spelling pubmed-80084472021-03-31 Interaction with Human Serum Proteins Reveals Biocompatibility of Phosphocholine-Functionalized SPIONs and Formation of Albumin-Decorated Nanoparticles Russo Krauss, Irene Picariello, Alessandra Vitiello, Giuseppe De Santis, Augusta Koutsioubas, Alexandros Houston, Judith E. Fragneto, Giovanna Paduano, Luigi Langmuir [Image: see text] 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. American Chemical Society 2020-06-23 2020-08-04 /pmc/articles/PMC8008447/ /pubmed/32575987 http://dx.doi.org/10.1021/acs.langmuir.0c01083 Text en Permits the broadest form of re-use including for commercial purposes, provided that author attribution and integrity are maintained (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Russo Krauss, Irene
Picariello, Alessandra
Vitiello, Giuseppe
De Santis, Augusta
Koutsioubas, Alexandros
Houston, Judith E.
Fragneto, Giovanna
Paduano, Luigi
Interaction with Human Serum Proteins Reveals Biocompatibility of Phosphocholine-Functionalized SPIONs and Formation of Albumin-Decorated Nanoparticles
title Interaction with Human Serum Proteins Reveals Biocompatibility of Phosphocholine-Functionalized SPIONs and Formation of Albumin-Decorated Nanoparticles
title_full Interaction with Human Serum Proteins Reveals Biocompatibility of Phosphocholine-Functionalized SPIONs and Formation of Albumin-Decorated Nanoparticles
title_fullStr Interaction with Human Serum Proteins Reveals Biocompatibility of Phosphocholine-Functionalized SPIONs and Formation of Albumin-Decorated Nanoparticles
title_full_unstemmed Interaction with Human Serum Proteins Reveals Biocompatibility of Phosphocholine-Functionalized SPIONs and Formation of Albumin-Decorated Nanoparticles
title_short Interaction with Human Serum Proteins Reveals Biocompatibility of Phosphocholine-Functionalized SPIONs and Formation of Albumin-Decorated Nanoparticles
title_sort interaction with human serum proteins reveals biocompatibility of phosphocholine-functionalized spions and formation of albumin-decorated nanoparticles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8008447/
https://www.ncbi.nlm.nih.gov/pubmed/32575987
http://dx.doi.org/10.1021/acs.langmuir.0c01083
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