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Proteomics Analysis Reveals Distinct Corona Composition on Magnetic Nanoparticles with Different Surface Coatings: Implications for Interactions with Primary Human Macrophages

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      Abstract

      Superparamagnetic iron oxide nanoparticles (SPIONs) have emerged as promising contrast agents for magnetic resonance imaging. The influence of different surface coatings on the biocompatibility of SPIONs has been addressed, but the potential impact of the so-called corona of adsorbed proteins on the surface of SPIONs on their biological behavior is less well studied. Here, we determined the composition of the plasma protein corona on silica-coated versus dextran-coated SPIONs using mass spectrometry-based proteomics approaches. Notably, gene ontology (GO) enrichment analysis and Kyoto Encyclopedia of Genes and Genomes (KEGG) pathway analysis revealed distinct protein corona compositions for the two different SPIONs. Relaxivity of silica-coated SPIONs was modulated by the presence of a protein corona. Moreover, the viability of primary human monocyte-derived macrophages was influenced by the protein corona on silica-coated, but not dextran-coated SPIONs, and the protein corona promoted cellular uptake of silica-coated SPIONs, but did not affect internalization of dextran-coated SPIONs.

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      Most cited references 33

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      Understanding biophysicochemical interactions at the nano-bio interface.

      Rapid growth in nanotechnology is increasing the likelihood of engineered nanomaterials coming into contact with humans and the environment. Nanoparticles interacting with proteins, membranes, cells, DNA and organelles establish a series of nanoparticle/biological interfaces that depend on colloidal forces as well as dynamic biophysicochemical interactions. These interactions lead to the formation of protein coronas, particle wrapping, intracellular uptake and biocatalytic processes that could have biocompatible or bioadverse outcomes. For their part, the biomolecules may induce phase transformations, free energy releases, restructuring and dissolution at the nanomaterial surface. Probing these various interfaces allows the development of predictive relationships between structure and activity that are determined by nanomaterial properties such as size, shape, surface chemistry, roughness and surface coatings. This knowledge is important from the perspective of safe use of nanomaterials.
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        An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database.

        A method to correlate the uninterpreted tandem mass spectra of peptides produced under low energy (10-50 eV) collision conditions with amino acid sequences in the Genpept database has been developed. In this method the protein database is searched to identify linear amino acid sequences within a mass tolerance of ±1 u of the precursor ion molecular weight A cross-correlation function is then used to provide a measurement of similarity between the mass-to-charge ratios for the fragment ions predicted from amino acid sequences obtained from the database and the fragment ions observed in the tandem mass spectrum. In general, a difference greater than 0.1 between the normalized cross-correlation functions of the first- and second-ranked search results indicates a successful match between sequence and spectrum. Searches of species-specific protein databases with tandem mass spectra acquired from peptides obtained from the enzymatically digested total proteins of E. coli and S. cerevisiae cells allowed matching of the spectra to amino acid sequences within proteins of these organisms. The approach described in this manuscript provides a convenient method to interpret tandem mass spectra with known sequences in a protein database.
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          Synthesis and surface engineering of iron oxide nanoparticles for biomedical applications.

          Superparamagnetic iron oxide nanoparticles (SPION) with appropriate surface chemistry have been widely used experimentally for numerous in vivo applications such as magnetic resonance imaging contrast enhancement, tissue repair, immunoassay, detoxification of biological fluids, hyperthermia, drug delivery and in cell separation, etc. All these biomedical and bioengineering applications require that these nanoparticles have high magnetization values and size smaller than 100 nm with overall narrow particle size distribution, so that the particles have uniform physical and chemical properties. In addition, these applications need special surface coating of the magnetic particles, which has to be not only non-toxic and biocompatible but also allow a targetable delivery with particle localization in a specific area. To this end, most work in this field has been done in improving the biocompatibility of the materials, but only a few scientific investigations and developments have been carried out in improving the quality of magnetic particles, their size distribution, their shape and surface in addition to characterizing them to get a protocol for the quality control of these particles. Nature of surface coatings and their subsequent geometric arrangement on the nanoparticles determine not only the overall size of the colloid but also play a significant role in biokinetics and biodistribution of nanoparticles in the body. The types of specific coating, or derivatization, for these nanoparticles depend on the end application and should be chosen by keeping a particular application in mind, whether it be aimed at inflammation response or anti-cancer agents. Magnetic nanoparticles can bind to drugs, proteins, enzymes, antibodies, or nucleotides and can be directed to an organ, tissue, or tumour using an external magnetic field or can be heated in alternating magnetic fields for use in hyperthermia. This review discusses the synthetic chemistry, fluid stabilization and surface modification of superparamagnetic iron oxide nanoparticles, as well as their use for above biomedical applications.
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            Author and article information

            Affiliations
            [1 ]Division of Molecular Toxicology, Institute of Environmental Medicine, Karolinska Institutet, Stockholm, Sweden
            [2 ]Clinical Proteomics Mass Spectrometry, Department of Oncology-Pathology, Science for Life Laboratory, and Karolinska Institutet, Stockholm, Sweden
            [3 ]NMR and Molecular Imaging Laboratory, Department of General, Organic and Biomedical Chemistry, University of Mons, Mons, Belgium
            [4 ]Electron Microscopy Core Facility, Department of Laboratory Medicine, Karolinska Institutet, Stockholm, Sweden
            [5 ]Division of Metals & Health, Institute of Environmental Medicine, Karolinska Institutet, Stockholm, Sweden
            [6 ]Functional Materials Division, School of Information and Communication Technology, Royal Institute of Technology, Stockholm, Sweden
            RMIT University, AUSTRALIA
            Author notes

            Competing Interests: The authors have declared that no competing interests exist.

            Conceived and designed the experiments: BF MT. Performed the experiments: CV MP KH SL. Analyzed the data: CV PK BF MV JL MT. Contributed reagents/materials/analysis tools: CV PK MP MV JL BF MT. Wrote the paper: CV BF.

            [¤]

            Current address: Department of Applied Physics, Royal Institute of Technology, Stockholm, Sweden

            Contributors
            Role: Editor
            Journal
            PLoS One
            PLoS ONE
            plos
            plosone
            PLoS ONE
            Public Library of Science (San Francisco, CA USA )
            1932-6203
            7 October 2015
            2015
            : 10
            : 10
            26444829
            4596693
            10.1371/journal.pone.0129008
            PONE-D-14-50625
            (Editor)

            This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited

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            Figures: 5, Tables: 4, Pages: 20
            Product
            Funding
            This work was supported by Swedish Research Council for Environment, Agricultural Sciences and Spatial Planning (BF), the Swedish Cancer and Allergy Foundation (BF), the Swedish Cancer Society (JL), the Swedish Research Council (BF, JL), and the European Commission (FP7-NANOSOLUTIONS, grant agreement no. 309329) (BF) and FP7-eNANOMAPPER, grant agreement no. 604134) (BF). The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.
            Categories
            Research Article
            Custom metadata
            All relevant data are within the paper and its Supporting Information files. Additionally, all proteomics data generated in this study are deposited to the ProteomeXchange Consortium ( http://proteomecentral.proteomexchange.org) with the dataset identifier PXD000766.

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