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Volumn 11, Issue 5, 2015, Pages 828-840

Protein corona formation on magnetite nanoparticles: Effects of culture medium composition, and its consequences on superparamagnetic nanoparticle cytotoxicity

Author keywords

Interference; Protein corona; Serum; Superparamagnetic iron oxide nanoparticles (SPIONs); Surface characterization

Indexed keywords

ASSAYS; CELL CULTURE; DESORPTION; FOURIER TRANSFORM INFRARED SPECTROSCOPY; IRON OXIDES; MAGNETITE NANOPARTICLES; SECONDARY ION MASS SPECTROMETRY; SUPERPARAMAGNETISM; TOPOGRAPHY; WAVE INTERFERENCE;

EID: 84918557509     PISSN: 15507033     EISSN: 15507041     Source Type: Journal    
DOI: 10.1166/jbn.2015.2000     Document Type: Article
Times cited : (26)

References (74)
  • 1
    • 77956069605 scopus 로고    scopus 로고
    • Inorganic manufactured nanoparticles: How their physicochemical properties influence their biological effects in aqueous environments
    • M. Auffan, J. Y. Bottero, C. Chaneac, and J. Rose, Inorganic manufactured nanoparticles: How their physicochemical properties influence their biological effects in aqueous environments. Nanomedicine-Nanotechnology, Biology, and Medicine 5, 999 (2010).
    • (2010) Nanomedicine-Nanotechnology, Biology, and Medicine , vol.5 , pp. 999
    • Auffan, M.1    Bottero, J.Y.2    Chaneac, C.3    Rose, J.4
  • 2
    • 84867372750 scopus 로고    scopus 로고
    • Reactivity of inorganic nanoparticles in biological environments: Insights into nanotoxicity mechanisms
    • E. Casals, E. Gonzalez, and V. F. Puntes, Reactivity of inorganic nanoparticles in biological environments: Insights into nanotoxicity mechanisms. Journal of Physics D-Applied Physics 45, 443001 (2012).
    • (2012) Journal of Physics D-Applied Physics , vol.45 , pp. 443001
    • Casals, E.1    Gonzalez, E.2    Puntes, V.F.3
  • 3
    • 79951884309 scopus 로고    scopus 로고
    • Nanoparticle-based mass spectrometry for the analysis of biomolecules
    • C. K. Chiang, W. T. Chen, and H. T. Chang, Nanoparticle-based mass spectrometry for the analysis of biomolecules. Chem. Soc. Rev. 40, 1269 (2011).
    • (2011) Chem. Soc. Rev. , vol.40 , pp. 1269
    • Chiang, C.K.1    Chen, W.T.2    Chang, H.T.3
  • 5
    • 84868104372 scopus 로고    scopus 로고
    • Engineering nanomaterials for biomedical applications requires understanding the nano-bio interface: A perspective
    • J. E. Gagner, S. Shrivastava, X. Qian, J. S. Dordick, and R. W. Siegel, Engineering nanomaterials for biomedical applications requires understanding the nano-bio interface: A perspective. Journal of Physical Chemistry Letters 3, 3149 (2012).
    • (2012) Journal of Physical Chemistry Letters , vol.3 , pp. 3149
    • Gagner, J.E.1    Shrivastava, S.2    Qian, X.3    Dordick, J.S.4    Siegel, R.W.5
  • 6
    • 84861532376 scopus 로고    scopus 로고
    • Mobile precursor mediated protein adsorption on solid surfaces
    • A. Garland, L. Shen, and X. Y. Zhu, Mobile precursor mediated protein adsorption on solid surfaces. Prog. Surf. Sci. 87, 1 (2012).
    • (2012) Prog. Surf. Sci. , vol.87 , pp. 1
    • Garland, A.1    Shen, L.2    Zhu, X.Y.3
  • 7
    • 58149184031 scopus 로고    scopus 로고
    • Characterization of size, surface charge, and agglomeration state of nanoparticle dispersions for toxicological studies
    • J. K. Jiang, G. Oberdorster, and P. Biswas, Characterization of size, surface charge, and agglomeration state of nanoparticle dispersions for toxicological studies. J. Nanopart. Res. 11, 77 (2009).
    • (2009) J. Nanopart. Res. , vol.11 , pp. 77
    • Jiang, J.K.1    Oberdorster, G.2    Biswas, P.3
  • 9
    • 79954480999 scopus 로고    scopus 로고
    • Gold nanoparticles delivery in mammalian live cells: A critical review
    • R. Levy, U. Shaheen, Y. Cesbron, and V. See, Gold nanoparticles delivery in mammalian live cells: A critical review. Nano Reviews 1, 4889 (2010).
    • (2010) Nano Reviews , vol.1 , pp. 4889
    • Levy, R.1    Shaheen, U.2    Cesbron, Y.3    See, V.4
  • 10
    • 35349010059 scopus 로고    scopus 로고
    • The nanoparticle-protein complex as a biological entity; a complex fluids and surface science challenge for the 21st century
    • I. Lynch, T. CedervalL, M. Lundqvist, C. Cabaleiro-Lago, S. Linse, and K. A. Dawson, The nanoparticle-protein complex as a biological entity; a complex fluids and surface science challenge for the 21st century. Adv. Colloid Interface Sci. 134-135, 167 (2007).
    • (2007) Adv. Colloid Interface Sci. , vol.134-135 , pp. 167
    • Lynch, I.1    Cedervall, T.2    Lundqvist, M.3    Cabaleiro-Lago, C.4    Linse, S.5    Dawson, K.A.6
  • 11
    • 39749107963 scopus 로고    scopus 로고
    • Protein-nanoparticle interactions
    • I. Lynch and K. A. Dawson, Protein-nanoparticle interactions. Nano Today 3, 40 (2008).
    • (2008) Nano Today , vol.3 , pp. 40
    • Lynch, I.1    Dawson, K.A.2
  • 13
    • 80051488693 scopus 로고    scopus 로고
    • Nano meets biology: Structure and function at the nanoparticle interface
    • D. F. Moyano and V. M. Rotello, Nano meets biology: Structure and function at the nanoparticle interface. Langmuir 27, 10376 (2011).
    • (2011) Langmuir , vol.27 , pp. 10376
    • Moyano, D.F.1    Rotello, V.M.2
  • 16
    • 79951770246 scopus 로고    scopus 로고
    • Understanding protein adsorption phenomena at solid surfaces
    • M. Rabe, D. Verdes, and S. Seeger, Understanding protein adsorption phenomena at solid surfaces. Adv. Colloid Interface Sci. 162, 87 (2011).
    • (2011) Adv. Colloid Interface Sci. , vol.162 , pp. 87
    • Rabe, M.1    Verdes, D.2    Seeger, S.3
  • 18
    • 78649806814 scopus 로고    scopus 로고
    • Engineering the nanoparticleprotein interface: Applications and possibilities
    • S. Rana, Y. C. Yeh, and V. M. Rotello, Engineering the nanoparticleprotein interface: Applications and possibilities. Abbreviations Journal Names 14, 828 (2010).
    • (2010) Abbreviations Journal Names , vol.14 , pp. 828
    • Rana, S.1    Yeh, Y.C.2    Rotello, V.M.3
  • 19
    • 84862867927 scopus 로고    scopus 로고
    • Molecular interaction of proteins and peptides with nanoparticles
    • A. A. Shemetov, I. Nabiev, and A. Sukhanova, Molecular interaction of proteins and peptides with nanoparticles. ACS Nano 6, 4585 (2012).
    • (2012) ACS Nano , vol.6 , pp. 4585
    • Shemetov, A.A.1    Nabiev, I.2    Sukhanova, A.3
  • 20
    • 84856423834 scopus 로고    scopus 로고
    • Understanding and controlling the interaction of nanomaterials with proteins in a physiological environment
    • A. D. Walkey and W. C. Chan, Understanding and controlling the interaction of nanomaterials with proteins in a physiological environment. Chem. Soc. Rev. 41, 2780 (2012).
    • (2012) Chem. Soc. Rev. , vol.41 , pp. 2780
    • Walkey, A.D.1    Chan, W.C.2
  • 21
    • 84877718041 scopus 로고    scopus 로고
    • Adsorption of proteins to functional polymeric nanoparticles
    • N. Welsch, Y. Lu, J. Dzubiella, and M. Ballauff, Adsorption of proteins to functional polymeric nanoparticles. Polymer 54, 2835 (2013).
    • (2013) Polymer , vol.54 , pp. 2835
    • Welsch, N.1    Lu, Y.2    Dzubiella, J.3    Ballauff, M.4
  • 22
    • 84878099108 scopus 로고    scopus 로고
    • Biosafety and bioapplication of nanomaterials by designing protein-nanoparticle interactions
    • S. T. Yang, Y. Liu, Y. W. Wang, and A. Cao, Biosafety and bioapplication of nanomaterials by designing protein-nanoparticle interactions. Small 9, 1635 (2013).
    • (2013) Small , vol.9 , pp. 1635
    • Yang, S.T.1    Liu, Y.2    Wang, Y.W.3    Cao, A.4
  • 23
    • 84878103207 scopus 로고    scopus 로고
    • Pino Interfacing engineered nanoparticles with biological systems: Anticipating adverse nano-bio interactions
    • A. Pelaz, G. Charron, C. Pfeiffer, Y. Zhao, J. M. DE LA Fuente, X. J. Liang, W. J. Parak, and P. DEl pino, Interfacing engineered nanoparticles with biological systems: Anticipating adverse nano-bio interactions. Small 9, 1573 (2013).
    • (2013) Small , vol.9 , pp. 1573
    • Pelaz, A.1    Charron, G.2    Pfeiffer, C.3    Zhao, Y.4    De La Fuente, J.M.5    Liang, X.J.6    Parak, W.J.7    Del, P.8
  • 24
    • 84867919759 scopus 로고    scopus 로고
    • Core-shell nanoparticles as prodrugs: Possible cytotoxicological and biomedical impacts of batch-to-batch inconsistencies
    • R. Franca, X. F. Zhang, T. Veres, L. Yahia, and E. Sacher, Core-shell nanoparticles as prodrugs: Possible cytotoxicological and biomedical impacts of batch-to-batch inconsistencies. J. Colloid Interface Sci. 389, 292 (2013).
    • (2013) J. Colloid Interface Sci. , vol.389 , pp. 292
    • Franca, R.1    Zhang, X.F.2    Veres, T.3    Yahia, L.4    Sacher, E.5
  • 25
    • 84918533552 scopus 로고
    • Impact of polymer shell on the formation and time evolution of nanoparticle-protein corona. Colloids and Surfaces B: Biointerfaces 104, 213 26. V. N. Maiorov and G. M. Crippen, Contact potential that recognizes the correct folding of globular proteins
    • K. Natte, J. F. Friedrich, S. Wohlrab, J. Lutzki, R. von Klitzing, W. Österle, and G. Orts-Gil, Impact of polymer shell on the formation and time evolution of nanoparticle-protein corona. Colloids and Surfaces B: Biointerfaces 104, 213 26. V. N. Maiorov and G. M. Crippen, Contact potential that recognizes the correct folding of globular proteins. J. Mol. Biol. 227, 876 (1992).
    • (1992) J. Mol. Biol. , vol.227 , pp. 876
    • Natte, K.1    Friedrich, J.F.2    Wohlrab, S.3    Lutzki, J.4    Von Klitzing, R.5    Österle, W.6    Orts-Gil, G.7
  • 26
    • 77649270954 scopus 로고    scopus 로고
    • Size and shape of protein molecules at the nanometer level determined by sedimentation, gel filtration, and electron microscopy
    • H. P. Erickson, Size and shape of protein molecules at the nanometer level determined by sedimentation, gel filtration, and electron microscopy. Biol. Proc. Online 11, 32 (2009).
    • (2009) Biol. Proc. Online , vol.11 , pp. 32
    • Erickson, H.P.1
  • 27
    • 83355173910 scopus 로고    scopus 로고
    • Protein adsorption in three dimensions
    • E. A. Vogler, Protein adsorption in three dimensions. Biomaterials 33, 1201 (2012).
    • (2012) Biomaterials , vol.33 , pp. 1201
    • Vogler, E.A.1
  • 30
    • 79551663421 scopus 로고    scopus 로고
    • Nanoparticles in biological systems
    • W. J. Stark, Nanoparticles in biological systems. Angewandte Chemie 50, 1242 (2011).
    • (2011) Angewandte Chemie , vol.50 , pp. 1242
    • Stark, W.J.1
  • 31
    • 70249136214 scopus 로고    scopus 로고
    • Protein-nanoparticle interactions: What does the cell see?
    • I. Lynch, A. Salvati, and k. A. Dawson, Protein-nanoparticle interactions: What does the cell see? Nat. Nanotechnol. 4, 546 (2009).
    • (2009) Nat. Nanotechnol. , vol.4 , pp. 546
    • Lynch, I.1    Salvati, A.2    Dawson, K.A.3
  • 33
    • 84866019700 scopus 로고    scopus 로고
    • Interference of engineered nanoparticles with in vitro toxicity assays
    • A. Kroll, M. H. Pillukat, D. Hahn, and J. Schnekenburger, Interference of engineered nanoparticles with in vitro toxicity assays. Arch. Toxicol. 86, 1123 (2012).
    • (2012) Arch. Toxicol. , vol.86 , pp. 1123
    • Kroll, A.1    Pillukat, M.H.2    Hahn, D.3    Schnekenburger, J.4
  • 34
    • 0037442463 scopus 로고    scopus 로고
    • Interference in MTT cell viability assay in activated macrophage cell line
    • M. Pozzolini, S. Scarf, U. Benatti, and M. Giovine, Interference in MTT cell viability assay in activated macrophage cell line. Anal. Biochem. 313, 338 (2003).
    • (2003) Anal. Biochem. , vol.313 , pp. 338
    • Pozzolini, M.1    Scarf, S.2    Benatti, U.3    Giovine, M.4
  • 35
    • 58149267870 scopus 로고    scopus 로고
    • Limitations and relative utility of screening assays to assess engineered nanoparticle toxicity in a human cell line
    • N. A. Monteiro-Riviere, A. O. Inman, and L. W. Zhang, Limitations and relative utility of screening assays to assess engineered nanoparticle toxicity in a human cell line. Toxicol. Appl. Pharmacol. 234, 222 (2009).
    • (2009) Toxicol. Appl. Pharmacol. , vol.234 , pp. 222
    • Monteiro-Riviere, N.A.1    Inman, A.O.2    Zhang, L.W.3
  • 36
    • 77953764860 scopus 로고    scopus 로고
    • Confirmation of X-ray photoelectron spectroscopy peak attributions of nanoparticulate iron oxides, using symmetric peak component line shapes
    • S. Poulin, R. Franca, L. Moreau-Belanger, and E. Sacher, Confirmation of X-ray photoelectron spectroscopy peak attributions of nanoparticulate iron oxides, using symmetric peak component line shapes. Journal of Physical Chemistry C 114, 10711 (2010).
    • (2010) Journal of Physical Chemistry C , vol.114 , pp. 10711
    • Poulin, S.1    Franca, R.2    Moreau-Belanger, L.3    Sacher, E.4
  • 38
    • 68549111149 scopus 로고    scopus 로고
    • Effect of surface charge and agglomerate degree of magnetic iron oxide nanoparticles on KB cellular uptake in vitro
    • Y. Ge, Y. Zhang, J. Xia, M. Ma, S. He, F. Nie, and N. Gu, Effect of surface charge and agglomerate degree of magnetic iron oxide nanoparticles on KB cellular uptake in vitro. Colloids and Surfaces B, Biointerfaces 73, 294 (2009).
    • (2009) Colloids and Surfaces B, Biointerfaces , vol.73 , pp. 294
    • Ge, Y.1    Zhang, Y.2    Xia, J.3    Ma, M.4    He, S.5    Nie, F.6    Gu, N.7
  • 40
    • 4544255267 scopus 로고    scopus 로고
    • Biological effects of ultrafine model particles in human macrophages and epithelial cells in mono- and co-culture
    • R. Wottrich, S. Diabate, and H. F. Krug, Biological effects of ultrafine model particles in human macrophages and epithelial cells in mono- and co-culture. International Journal of Hygiene and Environmental Health 207, 353 (2004).
    • (2004) International Journal of Hygiene and Environmental Health , vol.207 , pp. 353
    • Wottrich, R.1    Diabate, S.2    Krug, H.F.3
  • 41
    • 84954358544 scopus 로고    scopus 로고
    • In vitro investigation of oxide nanoparticle and carbon nanotube toxicity and intracellular accumulation in a549 human pneumocytes
    • A. Simon-Deckers, B. Gouget, M. Mayne-L'hermite, N. Herlin- Boime, C. Reynaud, and M. Carriere, In vitro investigation of oxide nanoparticle and carbon nanotube toxicity and intracellular accumulation in a549 human pneumocytes. Toxicology 253, 137 (2008).
    • (2008) Toxicology , vol.253 , pp. 137
    • Simon-Deckers, A.1    Gouget, B.2    Mayne-L'hermite, M.3    Herlin-Boime, N.4    Reynaud, C.5    Carriere, M.6
  • 43
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein dye binding
    • M. M. Bradford, A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein dye binding. Anal. Biochem. 72, 248 (1976).
    • (1976) Anal. Biochem. , vol.72 , pp. 248
    • Bradford, M.M.1
  • 44
    • 0037426487 scopus 로고    scopus 로고
    • Incorporating alpha-allyl glucoside into polyacrylonitrile by water-phase precipitation copolymerization to reduce protein adsorption and cell adhesion
    • Z. K. Xu, R. Q. Kou, Z. M. Liu, F. Q. Nie, and Y. Y. Xu, Incorporating alpha-allyl glucoside into polyacrylonitrile by water-phase precipitation copolymerization to reduce protein adsorption and cell adhesion. Macromolecules 36, 2441 (2003).
    • (2003) Macromolecules , vol.36 , pp. 2441
    • Xu, Z.K.1    Kou, R.Q.2    Liu, Z.M.3    Nie, F.Q.4    Xu, Y.Y.5
  • 45
    • 9244246319 scopus 로고    scopus 로고
    • Bovine serum albumin adsorption onto colloidal al2o3 particles: A new model based on zeta potential and uv-vis measurements
    • K. Rezwan, L. P. Meier, M. Rezwan, J. Voros, M. Textor, and L. J. Gauckler, Bovine serum albumin adsorption onto colloidal al2o3 particles: A new model based on zeta potential and uv-vis measurements. Langmuir 20, 10055 (2004).
    • (2004) Langmuir , vol.20 , pp. 10055
    • Rezwan, K.1    Meier, L.P.2    Rezwan, M.3    Voros, J.4    Textor, M.5    Gauckler, L.J.6
  • 46
    • 16344387506 scopus 로고    scopus 로고
    • Fibroblast cell behavior on bound and adsorbed fibronectin onto hyaluronan and sulfated hyaluronan substrates
    • R. Barbucci, A. Magnani, A. Chiumiento, D. Pasqui, I. Cangioli, and S. Lamponi, Fibroblast cell behavior on bound and adsorbed fibronectin onto hyaluronan and sulfated hyaluronan substrates. Biomacromolecules 6, 638 (2005).
    • (2005) Biomacromolecules , vol.6 , pp. 638
    • Barbucci, R.1    Magnani, A.2    Chiumiento, A.3    Pasqui, D.4    Cangioli, I.5    Lamponi, S.6
  • 48
    • 0033990815 scopus 로고    scopus 로고
    • Matrix-assisted laser desorption ionization mass spectrometry detection of proteins adsorbed in vivo onto contact lenses
    • P. Kingshott, H. A. W. St John, R. C. Chatelier, and H. J. Griesser, Matrix-assisted laser desorption ionization mass spectrometry detection of proteins adsorbed in vivo onto contact lenses. Journal of Biomedical Materials Research 49, 36 (2000).
    • (2000) Journal of Biomedical Materials Research , vol.49 , pp. 36
    • Kingshott, P.1    St John, H.A.W.2    Chatelier, R.C.3    Griesser, H.J.4
  • 51
    • 0021061819 scopus 로고
    • Rapid colorimetric assay for cellular growth and survival: Application to proliferation and cytotoxicity assays
    • T. Mosmann, Rapid colorimetric assay for cellular growth and survival: Application to proliferation and cytotoxicity assays. Journal of Immunological Methods 65, 55 (1983).
    • (1983) Journal of Immunological Methods , vol.65 , pp. 55
    • Mosmann, T.1
  • 52
    • 79951884309 scopus 로고    scopus 로고
    • Nanoparticle-based mass spectrometry for the analysis of biomolecules
    • A. K. Chiang, W. T. Chen, and H. T. Chang, Nanoparticle-based mass spectrometry for the analysis of biomolecules. Chem. Soc. Rev. 40, 1269 (2011).
    • (2011) Chem. Soc. Rev. , vol.40 , pp. 1269
    • Chiang, A.K.1    Chen, W.T.2    Chang, H.T.3
  • 54
    • 67651002623 scopus 로고    scopus 로고
    • PH-dependent surface charging and points of zero charge. IV. Update and new approach
    • M. Kosmulski, pH-dependent surface charging and points of zero charge. IV. Update and new approach. J. Colloid Interface Sci. 337, 439 (2009).
    • (2009) J. Colloid Interface Sci. , vol.337 , pp. 439
    • Kosmulski, M.1
  • 57
    • 38549165939 scopus 로고    scopus 로고
    • Proteins adsorption to orthopaedic biomaterials: Vibrational spectroscopy evidence
    • S. Cavalu and V. Simon, Proteins adsorption to orthopaedic biomaterials: Vibrational spectroscopy evidence. Journal of Optoelectronics and Advanced Materials 9, 3297 (2007).
    • (2007) Journal of Optoelectronics and Advanced Materials , vol.9 , pp. 3297
    • Cavalu, S.1    Simon, V.2
  • 59
    • 0018917567 scopus 로고
    • Interaction of high molecular weight kininogen, Factor XII and fibrinogen in plasma at interfaces
    • L. Vroman, A. L. Adams, G. C. Fisher, and P. C. Munoz, Interaction of high molecular weight kininogen, Factor XII and fibrinogen in plasma at interfaces. Blood 55, 156 (1980).
    • (1980) Blood , vol.55 , pp. 156
    • Vroman, L.1    Adams, A.L.2    Fisher, G.C.3    Munoz, P.C.4
  • 60
    • 0022078121 scopus 로고
    • Adsorption of proteins out of plasma and solutions in narrow spaces
    • L. Vroman and A. L. Adams, Adsorption of proteins out of plasma and solutions in narrow spaces. J. Colloid Interface Sci. 111, 391 (1986).
    • (1986) J. Colloid Interface Sci. , vol.111 , pp. 391
    • Vroman, L.1    Adams, A.L.2
  • 61
    • 0023468837 scopus 로고
    • Protein adsorption and materials biocompatibility: A tutorial review and suggested hypotheses
    • J. D. Andrade and V. Hlady, Protein adsorption and materials biocompatibility: A tutorial review and suggested hypotheses. Adv. Polym. Sci. 79, 1 (1986).
    • (1986) Adv. Polym. Sci. , vol.79 , pp. 1
    • Andrade, J.D.1    Hlady, V.2
  • 62
    • 0026038549 scopus 로고
    • Vroman effects, techniques and philosophies
    • J. D. Andrade and V. Hlady, Vroman effects, techniques and philosophies. J. Biomater. Sci. Polym. 2, 161 (1991).
    • (1991) J. Biomater. Sci. Polym. , vol.2 , pp. 161
    • Andrade, J.D.1    Hlady, V.2
  • 63
    • 39749107963 scopus 로고    scopus 로고
    • Protein-nanoparticle interactions
    • I. Lynch and K. A. Dawson, Protein-nanoparticle interactions. Nano Today 3, 40 (2008).
    • (2008) Nano Today , vol.3 , pp. 40
    • Lynch, I.1    Dawson, K.A.2
  • 65
    • 59949091290 scopus 로고    scopus 로고
    • Effects of proteins from culture medium on surface property of silanes-functionalized magnetic nanoparticles
    • Z. P. Chen, R. Z. Xu, Y. Zhang, and N. Gu, Effects of proteins from culture medium on surface property of silanes-functionalized magnetic nanoparticles. Nanoscale Research Letters 4, 204 (2009).
    • (2009) Nanoscale Research Letters , vol.4 , pp. 204
    • Chen, Z.P.1    Xu, R.Z.2    Zhang, Y.3    Gu, N.4
  • 66
    • 78650725684 scopus 로고    scopus 로고
    • Effects of cell culture media on the dynamic formation of protein-nanoparticle complexes and influence on the cellular response
    • G. Maiorano, S. Sabella, B. Sorce, V. Brunetti, M. A. Malvindi, R. Cingolani, and P. P. Pompa, Effects of cell culture media on the dynamic formation of protein-nanoparticle complexes and influence on the cellular response. Acs Nano 4, 7481 (2010).
    • (2010) Acs Nano , vol.4 , pp. 7481
    • Maiorano, G.1    Sabella, S.2    Sorce, B.3    Brunetti, V.4    Malvindi, M.A.5    Cingolani, R.6    Pompa, P.P.7
  • 68
    • 53549086404 scopus 로고    scopus 로고
    • Copper oxide nanoparticles are highly toxic: A comparison between metal oxide nanoparticles and carbon nanotubes
    • H. L. Karlsson, P. Cronholm, J. Gustafsson, and L. Moller, Copper oxide nanoparticles are highly toxic: A comparison between metal oxide nanoparticles and carbon nanotubes. Chemical Research in Toxicology, 21, 1726 (2008).
    • (2008) Chemical Research in Toxicology , vol.21 , pp. 1726
    • Karlsson, H.L.1    Cronholm, P.2    Gustafsson, J.3    Moller, L.4
  • 70
    • 57649221172 scopus 로고    scopus 로고
    • Discriminative cytotoxicity assessment based on various cellular damages
    • H. Kim, S. C. Yoon, T. Y. Lee, and D. Jeong, Discriminative cytotoxicity assessment based on various cellular damages. Toxicology Letters 184, 13 (2009).
    • (2009) Toxicology Letters , vol.184 , pp. 13
    • Kim, H.1    Yoon, S.C.2    Lee, T.Y.3    Jeong, D.4
  • 71
    • 84875863188 scopus 로고    scopus 로고
    • Protein corona formation for nanomaterials and proteins of a similar size: Hard or soft corona?
    • W. Liu, J. Rose, S. Plantevin, M. Auffan, J. Y. Bottero, and C. Vidaud, Protein corona formation for nanomaterials and proteins of a similar size: Hard or soft corona? Nanoscale 5, 1658 (2013).
    • (2013) Nanoscale , vol.5 , pp. 1658
    • Liu, W.1    Rose, J.2    Plantevin, S.3    Auffan, M.4    Bottero, J.Y.5    Vidaud, C.6
  • 72
    • 77949563772 scopus 로고    scopus 로고
    • Interactions between sub-10-nm iron and cerium oxide nanoparticles and 3T3 fibroblasts: The role of the coating and aggregation state
    • M. Safi, H. Sarrouj, O. Sandre, N. Mignet, and J. F. Berret, Interactions between sub-10-nm iron and cerium oxide nanoparticles and 3T3 fibroblasts: The role of the coating and aggregation state. Nanotechnology 21, 145103 (2010).
    • (2010) Nanotechnology , vol.21 , pp. 145103
    • Safi, M.1    Sarrouj, H.2    Sandre, O.3    Mignet, N.4    Berret, J.F.5
  • 73
    • 76549084812 scopus 로고    scopus 로고
    • Assay conditions can influence the outcome of cytotoxicity tests of nanomaterials: Better assay characterization is needed to compare studies
    • J. Geys, B. Nemery, and P. H. Hoet, Assay conditions can influence the outcome of cytotoxicity tests of nanomaterials: Better assay characterization is needed to compare studies. Toxicology in Vitro 24, 620 (2010).
    • (2010) Toxicology in Vitro , vol.24 , pp. 620
    • Geys, J.1    Nemery, B.2    Hoet, P.H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.