29
views
0
recommends
+1 Recommend
0 collections
    8
    shares
      • Record: found
      • Abstract: found
      • Article: found
      Is Open Access

      Dispersion of Nanoparticles in Different Media Importantly Determines the Composition of Their Protein Corona

      research-article

      Read this article at

      Bookmark
          There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.

          Abstract

          Protein corona of nanoparticles (NPs), which forms when these particles come in to contact with protein-containing fluids, is considered as an overlooked factor in nanomedicine. Through numerous studies it has been becoming increasingly evident that it importantly dictates the interaction of NPs with their surroundings. Several factors that determine the compositions of NPs protein corona have been identified in recent years, but one has remained largely ignored—the composition of media used for dispersion of NPs. Here, we determined the effect of dispersion media on the composition of protein corona of polyacrylic acid-coated cobalt ferrite NPs (PAA NPs) and silica NPs. Our results confirmed some of the basic premises such as NPs type-dependent specificity of the protein corona. But more importantly, we demonstrated the effect of the dispersion media on the protein corona composition. The differences between constituents of the media used for dispersion of NPs, such as divalent ions and macromolecules were responsible for the differences in protein corona composition formed in the presence of fetal bovine serum (FBS). Our results suggest that the protein corona composition is a complex function of the constituents present in the media used for dispersion of NPs. Regardless of the dispersion media and FBS concentration, majority of proteins from either PAA NPs or silica NPs coronas were involved in the process of transport and hemostasis. Interestingly, corona of silica NPs contained three complement system related proteins: complement factor H, complement C3 and complement C4 while PAA NPs bound only one immune system related protein, α-2-glycoprotein. Importantly, relative abundance of complement C3 protein in corona of silica NPs was increased when NPs were dispersed in NaCl, which further implies the relevance of dispersion media used to prepare NPs.

          Related collections

          Most cited references30

          • Record: found
          • Abstract: found
          • Article: not found

          Binding of blood proteins to carbon nanotubes reduces cytotoxicity.

          With the potential wide uses of nanoparticles such as carbon nanotubes in biomedical applications, and the growing concerns of nanotoxicity of these engineered nanoparticles, the importance of nanoparticle-protein interactions cannot be stressed enough. In this study, we use both experimental and theoretical approaches, including atomic force microscope images, fluorescence spectroscopy, CD, SDS-PAGE, and molecular dynamics simulations, to investigate the interactions of single-wall carbon nanotubes (SWCNTs) with human serum proteins, and find a competitive binding of these proteins with different adsorption capacity and packing modes. The π-π stacking interactions between SWCNTs and aromatic residues (Trp, Phe, Tyr) are found to play a critical role in determining their adsorption capacity. Additional cellular cytotoxicity assays, with human acute monocytic leukemia cell line and human umbilical vein endothelial cells, reveal that the competitive bindings of blood proteins on the SWCNT surface can greatly alter their cellular interaction pathways and result in much reduced cytotoxicity for these protein-coated SWCNTs, according to their respective adsorption capacity. These findings have shed light toward the design of safe carbon nanotube nanomaterials by comprehensive preconsideration of their interactions with human serum proteins.
            Bookmark
            • Record: found
            • Abstract: found
            • Article: not found

            Protein corona fingerprinting predicts the cellular interaction of gold and silver nanoparticles.

            Using quantitative models to predict the biological interactions of nanoparticles will accelerate the translation of nanotechnology. Here, we characterized the serum protein corona 'fingerprint' formed around a library of 105 surface-modified gold nanoparticles. Applying a bioinformatics-inspired approach, we developed a multivariate model that uses the protein corona fingerprint to predict cell association 50% more accurately than a model that uses parameters describing nanoparticle size, aggregation state, and surface charge. Our model implicates a set of hyaluronan-binding proteins as mediators of nanoparticle-cell interactions. This study establishes a framework for developing a comprehensive database of protein corona fingerprints and biological responses for multiple nanoparticle types. Such a database can be used to develop quantitative relationships that predict the biological responses to nanoparticles and will aid in uncovering the fundamental mechanisms of nano-bio interactions.
              Bookmark
              • Record: found
              • Abstract: found
              • Article: not found

              Nanoparticle size is a critical physicochemical determinant of the human blood plasma corona: a comprehensive quantitative proteomic analysis.

              In biological fluids, proteins associate with nanoparticles, leading to a protein "corona" defining the biological identity of the particle. However, a comprehensive knowledge of particle-guided protein fingerprints and their dependence on nanomaterial properties is incomplete. We studied the long-lived ("hard") blood plasma derived corona on monodispersed amorphous silica nanoparticles differing in size (20, 30, and 100 nm). Employing label-free liquid chromatography mass spectrometry, one- and two-dimensional gel electrophoresis, and immunoblotting the composition of the protein corona was analyzed not only qualitatively but also quantitatively. Detected proteins were bioinformatically classified according to their physicochemical and biological properties. Binding of the 125 identified proteins did not simply reflect their relative abundance in the plasma but revealed an enrichment of specific lipoproteins as well as proteins involved in coagulation and the complement pathway. In contrast, immunoglobulins and acute phase response proteins displayed a lower affinity for the particles. Protein decoration of the negatively charged particles did not correlate with protein size or charge, demonstrating that electrostatic effects alone are not the major driving force regulating the nanoparticle-protein interaction. Remarkably, even differences in particle size of only 10 nm significantly determined the nanoparticle corona, although no clear correlation with particle surface volume, protein size, or charge was evident. Particle size quantitatively influenced the particle's decoration with 37% of all identified proteins, including (patho)biologically relevant candidates. We demonstrate the complexity of the plasma corona and its still unresolved physicochemical regulation, which need to be considered in nanobioscience in the future. © 2011 American Chemical Society
                Bookmark

                Author and article information

                Contributors
                Role: Editor
                Journal
                PLoS One
                PLoS ONE
                plos
                plosone
                PLoS ONE
                Public Library of Science (San Francisco, CA USA )
                1932-6203
                4 January 2017
                2017
                : 12
                : 1
                : e0169552
                Affiliations
                [1 ]Group for nano and biotechnological applications, Faculty of Electrical Engineering, University of Ljubljana, Ljubljana, Slovenia
                [2 ]Department of Molecular and Biomedical Sciences, Jožef Stefan Institute, Ljubljana, Slovenia
                [3 ]Department of Chemistry and Biochemistry, Faculty of Chemistry and Chemical Technology, University of Ljubljana, Ljubljana, Slovenia
                [4 ]Department of Organic Chemistry, Faculty of Chemistry and Chemical Technology, University of Ljubljana, Ljubljana, Slovenia
                [5 ]Institute of Biophysics, Faculty of Medicine, University of Ljubljana, Ljubljana, Slovenia
                Brandeis University, UNITED STATES
                Author notes

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

                • Conceptualization: KS AL IK MP.

                • Data curation: KS.

                • Formal analysis: KS AL JS.

                • Investigation: KS AL VB.

                • Supervision: IK MP.

                • Visualization: KS.

                • Writing – original draft: KS AL IK MP.

                Article
                PONE-D-16-35098
                10.1371/journal.pone.0169552
                5215476
                28052135
                4b7b10d1-0a79-4814-bf68-3f3920b2e728
                © 2017 Strojan et al

                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.

                History
                : 1 September 2016
                : 19 December 2016
                Page count
                Figures: 6, Tables: 3, Pages: 21
                Funding
                Funded by: funder-id http://dx.doi.org/10.13039/501100004329, Javna Agencija za Raziskovalno Dejavnost RS;
                Award ID: J7-7424
                Award Recipient : Vladimir Boštjan B. Bregar
                Funded by: funder-id http://dx.doi.org/10.13039/501100004329, Javna Agencija za Raziskovalno Dejavnost RS;
                Award ID: J3-6794
                Award Recipient :
                Funded by: funder-id http://dx.doi.org/10.13039/501100004329, Javna Agencija za Raziskovalno Dejavnost RS;
                Award ID: J2-6758
                Award Recipient : Vladimir Boštjan B. Bregar
                Funded by: funder-id http://dx.doi.org/10.13039/501100004329, Javna Agencija za Raziskovalno Dejavnost RS;
                Award ID: P1-0055
                Award Recipient :
                Funded by: funder-id http://dx.doi.org/10.13039/501100004329, Javna Agencija za Raziskovalno Dejavnost RS;
                Award ID: P1-0207
                Award Recipient :
                Funded by: funder-id http://dx.doi.org/10.13039/501100004329, Javna Agencija za Raziskovalno Dejavnost RS;
                Award ID: Young Researcher Program
                Award Recipient :
                This study was supported by the Slovenian Research Agency (ARRS; www.arrs.gov.si) research grants #J3-6794, #J7-7424, #J2-6758, #P1-0055 and #P1-0207. K.S. was also supported by the ARRS young researcher programme. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.
                Categories
                Research Article
                Biology and Life Sciences
                Biochemistry
                Proteins
                Serum Proteins
                Biology and Life Sciences
                Immunology
                Immune System Proteins
                Medicine and Health Sciences
                Immunology
                Immune System Proteins
                Biology and Life Sciences
                Biochemistry
                Proteins
                Immune System Proteins
                Biology and Life Sciences
                Physiology
                Immune Physiology
                Complement System
                Medicine and Health Sciences
                Physiology
                Immune Physiology
                Complement System
                Biology and Life Sciences
                Immunology
                Immune System
                Complement System
                Medicine and Health Sciences
                Immunology
                Immune System
                Complement System
                Biology and Life Sciences
                Immunology
                Immune System Proteins
                Complement System
                Medicine and Health Sciences
                Immunology
                Immune System Proteins
                Complement System
                Biology and Life Sciences
                Biochemistry
                Proteins
                Immune System Proteins
                Complement System
                Biology and Life Sciences
                Biophysics
                Ion Transport
                Physical Sciences
                Physics
                Biophysics
                Ion Transport
                Research and Analysis Methods
                Bioassays and Physiological Analysis
                Transport Inhibition Assay
                Medicine and Health Sciences
                Endocrinology
                Endocrine Physiology
                Hormone Transport
                Biology and Life Sciences
                Physiology
                Endocrine Physiology
                Hormone Transport
                Medicine and Health Sciences
                Physiology
                Endocrine Physiology
                Hormone Transport
                Physical Sciences
                Physics
                Classical Mechanics
                Continuum Mechanics
                Fluid Mechanics
                Fluid Dynamics
                Hydrodynamics
                Physical Sciences
                Chemistry
                Chemical Elements
                Cobalt
                Custom metadata
                All relevant data are within the paper and its Supporting Information files.

                Uncategorized
                Uncategorized

                Comments

                Comment on this article