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Volumn 117, Issue 39, 2013, Pages 20320-20331

Magnetic nanoparticles with covalently bound self-assembled protein corona for advanced biomedical applications

Author keywords

[No Author keywords available]

Indexed keywords

BIOMEDICAL APPLICATIONS; BOVINE SERUM ALBUMINS; CELL CULTURE MEDIUMS; COLLOIDAL PROPERTIES; MAGHEMITE NANOPARTICLE; MAGNETIC NANO-PARTICLES; NANOPARTICLE SURFACE; SURFACE CHARACTERISTICS;

EID: 84885140491     PISSN: 19327447     EISSN: 19327455     Source Type: Journal    
DOI: 10.1021/jp4068137     Document Type: Article
Times cited : (65)

References (54)
  • 1
    • 84862864780 scopus 로고    scopus 로고
    • Magnetic Nanoparticle-Based Theranostics
    • Xie, J.; Jon, S. Magnetic Nanoparticle-Based Theranostics Theranostics 2012, 2, 122-124
    • (2012) Theranostics , vol.2 , pp. 122-124
    • Xie, J.1    Jon, S.2
  • 2
    • 27644542061 scopus 로고    scopus 로고
    • Medical Application of Functionalized Magnetic Nanoparticles
    • Ito, A.; Shinkai, M.; Honda, H.; Kobayashi, T. Medical Application of Functionalized Magnetic Nanoparticles J. Biosci. Bioeng. 2005, 100, 1-11
    • (2005) J. Biosci. Bioeng. , vol.100 , pp. 1-11
    • Ito, A.1    Shinkai, M.2    Honda, H.3    Kobayashi, T.4
  • 3
    • 84868122898 scopus 로고    scopus 로고
    • Avidin Functionalized Maghemite Nanoparticles and their Application for Recombinant Human Biotinyl-SERCA Purification
    • Magro, M.; Faralli, A.; Baratella, D.; Bertipaglia, I.; Giannetti, S.; Salviulo, G.; Zboril, R.; Vianello, F. Avidin Functionalized Maghemite Nanoparticles and their Application for Recombinant Human Biotinyl-SERCA Purification Langmuir 2012, 28, 15392-15401
    • (2012) Langmuir , vol.28 , pp. 15392-15401
    • Magro, M.1    Faralli, A.2    Baratella, D.3    Bertipaglia, I.4    Giannetti, S.5    Salviulo, G.6    Zboril, R.7    Vianello, F.8
  • 4
    • 0034683143 scopus 로고    scopus 로고
    • Application of Magnetite and Silica-Magnetite Composites to the Isolation of Genomic DNA
    • Taylor, J. I.; Hurst, C. D.; Davies, M. J.; Sachsinger, N.; Bruce, I. J. Application of Magnetite and Silica-Magnetite Composites to the Isolation of Genomic DNA J. Chromatogr., A 2000, 890, 159-166
    • (2000) J. Chromatogr., A , vol.890 , pp. 159-166
    • Taylor, J.I.1    Hurst, C.D.2    Davies, M.J.3    Sachsinger, N.4    Bruce, I.J.5
  • 5
    • 1442348876 scopus 로고    scopus 로고
    • Magnetite-Containing Spherical Silica Nanoparticles for Biocatalysis and Bioseparations
    • Yang, H. H.; Zhang, S. Q.; Chen, X. L.; Zhuang, Z. X.; Xu, J. G.; Wang, X. R. Magnetite-Containing Spherical Silica Nanoparticles for Biocatalysis and Bioseparations Anal. Chem. 2004, 76, 1316-1321
    • (2004) Anal. Chem. , vol.76 , pp. 1316-1321
    • Yang, H.H.1    Zhang, S.Q.2    Chen, X.L.3    Zhuang, Z.X.4    Xu, J.G.5    Wang, X.R.6
  • 6
    • 18144377999 scopus 로고    scopus 로고
    • Superparamagnetic Nanoparticles for Biomedical Applications: Possibilities and Limitations of a New Drug Delivery System
    • Neuberger, T.; Schopf, B.; Hofmann, H.; Hofmann, M.; Rechenberg, B. V. Superparamagnetic Nanoparticles for Biomedical Applications: Possibilities and Limitations of a New Drug Delivery System J. Magn. Magn. Mater. 2005, 293, 483-496
    • (2005) J. Magn. Magn. Mater. , vol.293 , pp. 483-496
    • Neuberger, T.1    Schopf, B.2    Hofmann, H.3    Hofmann, M.4    Rechenberg, B.V.5
  • 7
    • 79960231793 scopus 로고    scopus 로고
    • Magnetic Nanomaterials for Hyperthermia-Based Therapy and Controlled Drug Delivery
    • Kumar, C. S.; Mohammad, F. Magnetic Nanomaterials for Hyperthermia-Based Therapy and Controlled Drug Delivery Adv. Drug Delivery Rev. 2011, 63, 789-808
    • (2011) Adv. Drug Delivery Rev. , vol.63 , pp. 789-808
    • Kumar, C.S.1    Mohammad, F.2
  • 9
    • 84860917662 scopus 로고    scopus 로고
    • Improving the Magnetic Resonance Imaging Contrast and Detection Methods with Engineered Magnetic Nanoparticles
    • Huang, J.; Zhong, X.; Wang, L.; Yang, L.; Mao, H. Improving the Magnetic Resonance Imaging Contrast and Detection Methods with Engineered Magnetic Nanoparticles Theranostics 2012, 2, 86-102
    • (2012) Theranostics , vol.2 , pp. 86-102
    • Huang, J.1    Zhong, X.2    Wang, L.3    Yang, L.4    Mao, H.5
  • 10
    • 47249140441 scopus 로고    scopus 로고
    • Magnetic Iron Oxide Nanoparticles: Synthesis, Stabilization, Vectorization, Physicochemical Characterizations, and Biological Applications
    • Laurent, S.; Forge, D.; Port, M.; Roch, A.; Robic, C.; Vander Elst, L.; Muller, R. N. Magnetic Iron Oxide Nanoparticles: Synthesis, Stabilization, Vectorization, Physicochemical Characterizations, and Biological Applications Chem. Rev. 2008, 108, 2064-2110
    • (2008) Chem. Rev. , vol.108 , pp. 2064-2110
    • Laurent, S.1    Forge, D.2    Port, M.3    Roch, A.4    Robic, C.5    Vander Elst, L.6    Muller, R.N.7
  • 11
    • 78149308762 scopus 로고    scopus 로고
    • Assessing Iron Oxide Nanoparticle Toxicity in Vitro: Current Status and Future Prospects
    • Soenen, S. J.; De Cuyper, M. Assessing Iron Oxide Nanoparticle Toxicity in Vitro: Current Status and Future Prospects Nanomedicine (London, U.K.) 2010, 5, 1261-1275
    • (2010) Nanomedicine (London, U.K.) , vol.5 , pp. 1261-1275
    • Soenen, S.J.1    De Cuyper, M.2
  • 12
    • 84857501798 scopus 로고    scopus 로고
    • Potential Applications of Enzymes Immobilized on/in Nano Materials: A Review
    • Ansari, S. A.; Husain, Q. Potential Applications of Enzymes Immobilized on/in Nano Materials: A Review Biotechnol. Adv. 2012, 30, 512-523
    • (2012) Biotechnol. Adv. , vol.30 , pp. 512-523
    • Ansari, S.A.1    Husain, Q.2
  • 16
    • 65749117793 scopus 로고    scopus 로고
    • Nanoparticle Interaction with Plasma Proteins as it Relates to Particle Biodistribution, Biocompatibility and Therapeutic Efficacy
    • Aggarwal, P.; Hall, J. B.; McLeland, C. B.; Dobrovolskaia, M. A.; McNeil, S. E. Nanoparticle Interaction with Plasma Proteins as it Relates to Particle Biodistribution, Biocompatibility and Therapeutic Efficacy Adv. Drug Delivery Rev. 2009, 61, 428-437
    • (2009) Adv. Drug Delivery Rev. , vol.61 , pp. 428-437
    • Aggarwal, P.1    Hall, J.B.2    McLeland, C.B.3    Dobrovolskaia, M.A.4    McNeil, S.E.5
  • 17
    • 0030592163 scopus 로고    scopus 로고
    • Characterization of Site i on Human Serum Albumin: Concept about the Structure of a Drug Binding Site
    • Yamasaki, K.; Maruyama, T.; Kragh-Hansen, U.; Otagiri, M. Characterization of Site I on Human Serum Albumin: Concept About the Structure of a Drug Binding Site Biochim. Biophys. Acta 1996, 1295, 147-157
    • (1996) Biochim. Biophys. Acta , vol.1295 , pp. 147-157
    • Yamasaki, K.1    Maruyama, T.2    Kragh-Hansen, U.3    Otagiri, M.4
  • 19
    • 51449088432 scopus 로고    scopus 로고
    • Investigation on Damage of BSA Molecules under Irradiation of Low Frequency Ultrasound in the Presence of FeIII-Tartrate Complexes
    • Wang, J.; Wang, Y.; Gao, J.; Hu, P.; Guan, H.; Zhang, L.; Xu, R.; Chen, X.; Zhang, X. Investigation on Damage of BSA Molecules Under Irradiation of Low Frequency Ultrasound in the Presence of FeIII-Tartrate Complexes Ultrason. Sonochem. 2009, 16, 41-49
    • (2009) Ultrason. Sonochem. , vol.16 , pp. 41-49
    • Wang, J.1    Wang, Y.2    Gao, J.3    Hu, P.4    Guan, H.5    Zhang, L.6    Xu, R.7    Chen, X.8    Zhang, X.9
  • 20
    • 0019538149 scopus 로고
    • Molecular Aspects of Ligand Binding to Serum Albumin
    • Kragh-Hansen, U. Molecular Aspects of Ligand Binding to Serum Albumin Pharmacol. Rev. 1981, 33, 17-53
    • (1981) Pharmacol. Rev. , vol.33 , pp. 17-53
    • Kragh-Hansen, U.1
  • 24
    • 0032818805 scopus 로고    scopus 로고
    • FTIR Spectroscopic Characterization of Protein Structure in Aqueous and non-Aqueous Media
    • Harris, P. I.; Severcan, F. FTIR Spectroscopic Characterization of Protein Structure in Aqueous and non-Aqueous Media J. Mol. Catal. B: Enzym. 1999, 7, 207-221
    • (1999) J. Mol. Catal. B: Enzym. , vol.7 , pp. 207-221
    • Harris, P.I.1    Severcan, F.2
  • 25
    • 84865790649 scopus 로고    scopus 로고
    • How Do Proteins Unfold Upon Adsorption on Nanoparticle Surfaces?
    • Pan, H.; Qin, M.; Meng, W.; Cao, Y.; Wang, W. How Do Proteins Unfold Upon Adsorption on Nanoparticle Surfaces? Langmuir 2012, 28, 12779-12787
    • (2012) Langmuir , vol.28 , pp. 12779-12787
    • Pan, H.1    Qin, M.2    Meng, W.3    Cao, Y.4    Wang, W.5
  • 26
    • 79952668032 scopus 로고    scopus 로고
    • Irreversible Changes in Protein Conformation Due to Interaction with Superparamagnetic Iron Oxide Nanoparticles
    • Mahmoudi, M.; Shokrgozar, M. A.; Sardari, S.; Moghadam, M. K.; Vali, H.; Laurent, S.; Stroeve, P. Irreversible Changes in Protein Conformation Due to Interaction with Superparamagnetic Iron Oxide Nanoparticles Nanoscale 2011, 3, 1127-1138
    • (2011) Nanoscale , vol.3 , pp. 1127-1138
    • Mahmoudi, M.1    Shokrgozar, M.A.2    Sardari, S.3    Moghadam, M.K.4    Vali, H.5    Laurent, S.6    Stroeve, P.7
  • 27
    • 65249178901 scopus 로고    scopus 로고
    • Immobilization of BSA on Silica-Coated Magnetic Iron Oxide Nanoparticle
    • Yu, C. H.; Al-Saadi, A.; Shih, S. J.; Qiu, L.; Tam, K. Y.; Tsang, S. C. Immobilization of BSA on Silica-Coated Magnetic Iron Oxide Nanoparticle J. Phys. Chem. C 2009, 113, 537-543
    • (2009) J. Phys. Chem. C , vol.113 , pp. 537-543
    • Yu, C.H.1    Al-Saadi, A.2    Shih, S.J.3    Qiu, L.4    Tam, K.Y.5    Tsang, S.C.6
  • 28
    • 33745457636 scopus 로고    scopus 로고
    • Fabrication of Protein-Conjugated Silver Sulfide Nanorods in the Bovine Serum Albumin Solution
    • Yang, L.; Xing, R.; Shen, Q.; Jiang, K.; Ye, F.; Wang, J.; Ren, Q. Fabrication of Protein-Conjugated Silver Sulfide Nanorods in the Bovine Serum Albumin Solution J. Phys. Chem. B 2006, 110, 10534-10539
    • (2006) J. Phys. Chem. B , vol.110 , pp. 10534-10539
    • Yang, L.1    Xing, R.2    Shen, Q.3    Jiang, K.4    Ye, F.5    Wang, J.6    Ren, Q.7
  • 30
    • 70249136214 scopus 로고    scopus 로고
    • Protein-Nanoparticle Interactions: What Does the Cell See?
    • Lynch, I.; Salvati, A.; Dawson, K. A. Protein-Nanoparticle Interactions: What Does the Cell See? Nat. Nanotechnol 2009, 4, 546-547
    • (2009) Nat. Nanotechnol , vol.4 , pp. 546-547
    • Lynch, I.1    Salvati, A.2    Dawson, K.A.3
  • 31
    • 33646183969 scopus 로고    scopus 로고
    • Detecting Cryptic Epitopes Created by Nanoparticles
    • Lynch, I.; Dawson, K. A.; Linse, S. Detecting Cryptic Epitopes Created by Nanoparticles Sci. STKE 2006, 327 (pe14) 1-6
    • (2006) Sci. STKE , vol.327 , Issue.PE14 , pp. 1-6
    • Lynch, I.1    Dawson, K.A.2    Linse, S.3
  • 33
    • 84857879296 scopus 로고    scopus 로고
    • Insight into Serum Protein Interactions with Functionalized Magnetic Nanoparticles in Biological Media
    • Wiogo, H. T.; Lim, M.; Bulmus, V.; Gutierrez, L.; Woodward, R. C.; Amal, R. Insight into Serum Protein Interactions with Functionalized Magnetic Nanoparticles in Biological Media Langmuir 2012, 28, 4346-4356
    • (2012) Langmuir , vol.28 , pp. 4346-4356
    • Wiogo, H.T.1    Lim, M.2    Bulmus, V.3    Gutierrez, L.4    Woodward, R.C.5    Amal, R.6
  • 35
    • 23944492134 scopus 로고    scopus 로고
    • Overview of the HUPO Plasma Proteome Project: Results from the pilot phase with 35 collaborating laboratories and multiple analytical groups, generating a core dataset of 3020 proteins and a publicly available database.
    • Omenn, G. S.; States, D. J.; Adamski, M.; Blackwell, T. W.; Menon, R.; Hermjakob, H. Overview of the HUPO Plasma Proteome Project: results from the pilot phase with 35 collaborating laboratories and multiple analytical groups, generating a core dataset of 3020 proteins and a publicly available database. Proteomics 2005, 5, 3226-3245
    • (2005) Proteomics , vol.5 , pp. 3226-3245
    • Omenn, G.S.1    States, D.J.2    Adamski, M.3    Blackwell, T.W.4    Menon, R.5    Hermjakob, H.6
  • 36
    • 32144450818 scopus 로고    scopus 로고
    • Characterization of Regulatory Volume Behavior by Fluorescence Quenching in Human Corneal Epithelial Cells
    • Capo-Aponte, J. E.; Iserovich, P.; Reinach, P. S. Characterization of Regulatory Volume Behavior by Fluorescence Quenching in Human Corneal Epithelial Cells J. Membr. Biol. 2005, 207, 11-22
    • (2005) J. Membr. Biol. , vol.207 , pp. 11-22
    • Capo-Aponte, J.E.1    Iserovich, P.2    Reinach, P.S.3
  • 37
    • 80052858362 scopus 로고    scopus 로고
    • The Internalization Pathway, Metabolic Fate and Biological Effect of Superparamagnetic Iron Oxide Nanoparticles in the Macrophage-Like RAW264.7 Cell
    • Gu, J.; Xu, H.; Han, Y.; Dai, W.; Hao, W.; Wang, C.; Gu, N.; Xu, H.; Cao, J. The Internalization Pathway, Metabolic Fate and Biological Effect of Superparamagnetic Iron Oxide Nanoparticles in the Macrophage-Like RAW264.7 Cell Sci. China: Life Sci. 2011, 54, 793-805
    • (2011) Sci. China: Life Sci. , vol.54 , pp. 793-805
    • Gu, J.1    Xu, H.2    Han, Y.3    Dai, W.4    Hao, W.5    Wang, C.6    Gu, N.7    Xu, H.8    Cao, J.9
  • 38
    • 0019480519 scopus 로고
    • Monitoring of Relative Mitochondrial Membrane Potential in Living Cells by Fluorescence Microscopy
    • Johnson, L. V.; Walsh, M. L.; Bockus, B. J.; Chen, L. B. Monitoring of Relative Mitochondrial Membrane Potential in Living Cells by Fluorescence Microscopy J. Cell. Biol. 1981, 88, 526-535
    • (1981) J. Cell. Biol. , vol.88 , pp. 526-535
    • Johnson, L.V.1    Walsh, M.L.2    Bockus, B.J.3    Chen, L.B.4
  • 39
    • 84864833730 scopus 로고    scopus 로고
    • Detection of TiO2 Nanoparticles in Cells by Flow Cytometry
    • Zucker, R. M.; Daniel, K. M. Detection of TiO2 Nanoparticles in Cells by Flow Cytometry Methods Mol. Biol. 2010, 906, 497-509
    • (2010) Methods Mol. Biol. , vol.906 , pp. 497-509
    • Zucker, R.M.1    Daniel, K.M.2
  • 42
    • 0023738916 scopus 로고
    • A Quick and Simple Method for the Quantitation of Lactate Dehydrogenase Release in Measurements of Cellular Cytotoxicity and Tumor Necrosis Factor (TNF) Activity
    • Decker, T.; Lohmann-Matthes, M. L. A Quick and Simple Method for the Quantitation of Lactate Dehydrogenase Release in Measurements of Cellular Cytotoxicity and Tumor Necrosis Factor (TNF) Activity J. Immunol. Methods 1988, 115, 61-69
    • (1988) J. Immunol. Methods , vol.115 , pp. 61-69
    • Decker, T.1    Lohmann-Matthes, M.L.2
  • 43
    • 20644449754 scopus 로고    scopus 로고
    • Nanotoxicology: An Emerging Discipline Evolving from Studies of Ultrafine Particles
    • Oberdorster, G.; Oberdorster, E.; Oberdorster, J. Nanotoxicology: an Emerging Discipline Evolving from Studies of Ultrafine Particles Environ. Health Perspect. 2005, 113, 823-839
    • (2005) Environ. Health Perspect. , vol.113 , pp. 823-839
    • Oberdorster, G.1    Oberdorster, E.2    Oberdorster, J.3
  • 44
    • 28244481785 scopus 로고    scopus 로고
    • Oxidative Stress-Induced DNA Damage by Particulate Air Pollution
    • Risom, L.; Moller, P.; Loft, S. Oxidative Stress-Induced DNA Damage by Particulate Air Pollution Mutat. Res. 2005, 592, 119-137
    • (2005) Mutat. Res. , vol.592 , pp. 119-137
    • Risom, L.1    Moller, P.2    Loft, S.3
  • 45
    • 13244273521 scopus 로고    scopus 로고
    • Multiparametric Characterization by Flow Cytometry of Flow-Sorted Subpopulations of a Human Hepatoma Cell Line Useful for Drug Research
    • O'Connor, J. E.; Martinez, A.; Castell, J. V.; Gomez-Lechon, M. J. Multiparametric Characterization by Flow Cytometry of Flow-Sorted Subpopulations of a Human Hepatoma Cell Line Useful for Drug Research Cytometry, Part A 2005, 63, 48-58
    • (2005) Cytometry, Part A , vol.63 , pp. 48-58
    • O'Connor, J.E.1    Martinez, A.2    Castell, J.V.3    Gomez-Lechon, M.J.4
  • 46
    • 0024361491 scopus 로고
    • Effects of in Vivo and in Vitro Exposure to Rhodamine Dyes on Mitochondrial Function of Mouse Embryos
    • Ranganathan, S.; Hood, R. D. Effects of In Vivo and In Vitro Exposure to Rhodamine Dyes on Mitochondrial Function of Mouse Embryos Teratog., Carcinog., Mutagen. 1989, 9, 29-37
    • (1989) Teratog., Carcinog., Mutagen. , vol.9 , pp. 29-37
    • Ranganathan, S.1    Hood, R.D.2
  • 47
    • 0024384941 scopus 로고
    • Reduction of G1 Phase Duration and Enhancement of c-myc Gene Expression in HeLa Cells at Hypergravity
    • Kumei, Y.; Nakajima, T.; Sato, A.; Kamata, N.; Enomoto, S. Reduction of G1 Phase Duration and Enhancement of c-myc Gene Expression in HeLa Cells at Hypergravity J. Cell. Science 1989, 93, 221-226
    • (1989) J. Cell. Science , vol.93 , pp. 221-226
    • Kumei, Y.1    Nakajima, T.2    Sato, A.3    Kamata, N.4    Enomoto, S.5
  • 48
    • 0346949029 scopus 로고    scopus 로고
    • Competitive Adsorption of Serum Proteins at Microparticles Affects Phagocytosis by Dendritic Cells
    • Thiele, L.; Diederichs, J. E.; Reszka, R.; Merkle, H. P.; Walter, E. Competitive Adsorption of Serum Proteins at Microparticles Affects Phagocytosis by Dendritic Cells Biomaterials 2003, 24, 1409-1418
    • (2003) Biomaterials , vol.24 , pp. 1409-1418
    • Thiele, L.1    Diederichs, J.E.2    Reszka, R.3    Merkle, H.P.4    Walter, E.5
  • 49
    • 84864139993 scopus 로고    scopus 로고
    • Biomimetic Delivery with Micro- and Nanoparticles
    • Balmert, S. C.; Little, S. R. Biomimetic Delivery with Micro- and Nanoparticles Adv. Mater. 2012, 24, 3757-3778
    • (2012) Adv. Mater. , vol.24 , pp. 3757-3778
    • Balmert, S.C.1    Little, S.R.2
  • 50
    • 0041374239 scopus 로고    scopus 로고
    • Fetuin/Alpha2-HS Glycoprotein Enhances Phagocytosis of Apoptotic Cells and Macropinocytosis by Human Macrophages
    • Jersmann, H. P.; Dransfield, I.; Hart, S. P. Fetuin/Alpha2-HS Glycoprotein Enhances Phagocytosis of Apoptotic Cells and Macropinocytosis by Human Macrophages Clin. Sci. 2003, 105, 273-278
    • (2003) Clin. Sci. , vol.105 , pp. 273-278
    • Jersmann, H.P.1    Dransfield, I.2    Hart, S.P.3
  • 51
    • 84874624831 scopus 로고    scopus 로고
    • Protein Corona Significantly Reduces Active Targeting Yield
    • Mirshafiee, V.; Mahmoudi, M.; Lou, K.; Cheng, J.; Kraft, M. L. Protein Corona Significantly Reduces Active Targeting Yield Chem. Commun. 2013, 49, 2557-2559
    • (2013) Chem. Commun. , vol.49 , pp. 2557-2559
    • Mirshafiee, V.1    Mahmoudi, M.2    Lou, K.3    Cheng, J.4    Kraft, M.L.5


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