메뉴 건너뛰기




Volumn 9, Issue 9, 2014, Pages 2030-2044

Quantitative profiling of the protein coronas that form around nanoparticles

Author keywords

[No Author keywords available]

Indexed keywords

NANOPARTICLE; POLYSTYRENE DERIVATIVE; PROTEIN; SILICON DIOXIDE; SUCROSE; TRYPSIN;

EID: 84907029383     PISSN: 17542189     EISSN: 17502799     Source Type: Journal    
DOI: 10.1038/nprot.2014.139     Document Type: Article
Times cited : (213)

References (51)
  • 1
    • 84894412716 scopus 로고    scopus 로고
    • Nanotechnology: Using co-regulation to bring regulation of modern technologies into the 21st century
    • Reese, M. Nanotechnology: using co-regulation to bring regulation of modern technologies into the 21st century. Health Matrix Clevel. 23, 537-572 (2013).
    • (2013) Health Matrix Clevel. , vol.23 , pp. 537-572
    • Reese, M.1
  • 2
    • 84875924997 scopus 로고    scopus 로고
    • Interview: Nanomedicine: Past, present and future
    • Webster, T.J. Interview: Nanomedicine: past, present and future. Nanomedicine (Lond.) 8, 525-529 (2013).
    • (2013) Nanomedicine (Lond.) , vol.8 , pp. 525-529
    • Webster, T.J.1
  • 3
    • 84862682458 scopus 로고    scopus 로고
    • Safety assessment of nanomaterials: Implications for nanomedicine
    • Nystrom, A.M. & Fadeel, B. Safety assessment of nanomaterials: implications for nanomedicine. J. Control Release 161, 403-408 (2012).
    • (2012) J. Control Release , vol.161 , pp. 403-408
    • Nystrom, A.M.1    Fadeel, B.2
  • 4
    • 84930472195 scopus 로고    scopus 로고
    • Nanotoxicology: In vitro-in vivo dosimetry
    • Oberdorster, G. Nanotoxicology: in vitro-in vivo dosimetry. Environ. Health Perspect. 120, A13 (2012).
    • (2012) Environ. Health Perspect. , vol.120
    • Oberdorster, G.1
  • 5
    • 84885116495 scopus 로고    scopus 로고
    • The European Commission's recommendation on the definition of nanomaterial makes an impact
    • Rauscher, H., Sokull-Kluttgen, B. & Stamm, H. The European Commission's recommendation on the definition of nanomaterial makes an impact. Nanotoxicology 7, 1195-1197 (2013).
    • (2013) Nanotoxicology , vol.7 , pp. 1195-1197
    • Rauscher, H.1    Sokull-Kluttgen, B.2    Stamm, H.3
  • 6
    • 84873853768 scopus 로고    scopus 로고
    • Biomolecular coronas provide the biological identity of nanosized materials
    • Monopoli, M.P., Aberg, C., Salvati, A. & Dawson, K.A. Biomolecular coronas provide the biological identity of nanosized materials. Nat. Nanotechnol. 7, 779-786 (2012).
    • (2012) Nat. Nanotechnol. , vol.7 , pp. 779-786
    • Monopoli, M.P.1    Aberg, C.2    Salvati, A.3    Dawson, K.A.4
  • 8
    • 84885483569 scopus 로고    scopus 로고
    • Rapid formation of plasma protein corona critically affects nanoparticle pathophysiology
    • Tenzer, S. et al. Rapid formation of plasma protein corona critically affects nanoparticle pathophysiology. Nat. Nanotechnol. 8, 772-781 (2013).
    • (2013) Nat. Nanotechnol. , vol.8 , pp. 772-781
    • Tenzer, S.1
  • 9
    • 79960748365 scopus 로고    scopus 로고
    • DNA affects the composition of lipoplex protein corona: A proteomics approach
    • Capriotti, A.L. et al. DNA affects the composition of lipoplex protein corona: a proteomics approach. Proteomics 11, 3349-3358 (2012).
    • (2012) Proteomics , vol.11 , pp. 3349-3358
    • Capriotti, A.L.1
  • 10
    • 77956423135 scopus 로고    scopus 로고
    • An index for characterization of nanomaterials in biological systems
    • Xia, X.R., Monteiro-Riviere, N.A. & Riviere, J.E. An index for characterization of nanomaterials in biological systems. Nat. Nanotechnol. 5, 671-675 (2010).
    • (2010) Nat. Nanotechnol. , vol.5 , pp. 671-675
    • Xia, X.R.1    Monteiro-Riviere, N.A.2    Riviere, J.E.3
  • 11
    • 67649491055 scopus 로고    scopus 로고
    • Understanding biophysicochemical interactions at the nano-bio interface
    • Nel, A.E. et al. Understanding biophysicochemical interactions at the nano-bio interface. Nat. Mater. 8, 543-557 (2009).
    • (2009) Nat. Mater. , vol.8 , pp. 543-557
    • Nel, A.E.1
  • 12
    • 80053328840 scopus 로고    scopus 로고
    • Nanoparticle size is a critical physicochemical determinant of the human blood plasma corona: A comprehensive quantitative proteomic analysis
    • Tenzer, S. et al. Nanoparticle size is a critical physicochemical determinant of the human blood plasma corona: a comprehensive quantitative proteomic analysis. ACS Nano 5, 7155-7167 (2011).
    • (2011) ACS Nano , vol.5 , pp. 7155-7167
    • Tenzer, S.1
  • 13
    • 81855192707 scopus 로고    scopus 로고
    • Quantitative proteomics analysis of adsorbed plasma proteins classifies nanoparticles with different surface properties and size
    • Zhang, H. et al. Quantitative proteomics analysis of adsorbed plasma proteins classifies nanoparticles with different surface properties and size. Proteomics 11, 4569-4577 (2011).
    • (2011) Proteomics , vol.11 , pp. 4569-4577
    • Zhang, H.1
  • 14
    • 84873564939 scopus 로고    scopus 로고
    • Transferrin-functionalized nanoparticles lose their targeting capabilities when a biomolecule corona adsorbs on the surface
    • Salvati, A. et al. Transferrin-functionalized nanoparticles lose their targeting capabilities when a biomolecule corona adsorbs on the surface. Nat. Nanotechnol 8, 137-143 (2013).
    • (2013) Nat. Nanotechnol , vol.8 , pp. 137-143
    • Salvati, A.1
  • 15
    • 84883238627 scopus 로고    scopus 로고
    • Quantum dot-based Forster resonance energy transfer immunoassay for sensitive clinical diagnostics of low-volume serum samples
    • Wegner, K.D., Jin, Z., Linden, S., Jennings, T.L. & Hildebrandt, N. Quantum dot-based Forster resonance energy transfer immunoassay for sensitive clinical diagnostics of low-volume serum samples. ACS Nano 7, 7411-7419 (2013).
    • (2013) ACS Nano , vol.7 , pp. 7411-7419
    • Wegner, K.D.1    Jin, Z.2    Linden, S.3    Jennings, T.L.4    Hildebrandt, N.5
  • 16
    • 84885856023 scopus 로고    scopus 로고
    • Fabricated micro-nano devices for in vivo and in vitro biomedical applications
    • Barkam, S., Saraf, S. & Seal, S. Fabricated micro-nano devices for in vivo and in vitro biomedical applications. Wiley Interdiscip. Rev. Nanomed. Nanobiotechnol. 5, 544-568 (2013).
    • (2013) Wiley Interdiscip. Rev. Nanomed. Nanobiotechnol. , vol.5 , pp. 544-568
    • Barkam, S.1    Saraf, S.2    Seal, S.3
  • 18
    • 84895071750 scopus 로고    scopus 로고
    • Drift time-specific collision energies enable deep-coverage data-independent acquisition proteomics
    • Distler, U. et al. Drift time-specific collision energies enable deep-coverage data-independent acquisition proteomics. Nat. Methods 11, 167-170 (2014).
    • (2014) Nat. Methods , vol.11 , pp. 167-170
    • Distler, U.1
  • 19
    • 84889058853 scopus 로고    scopus 로고
    • Nanoparticulate flurbiprofen reduces amyloid-β42 generation in an in vitro blood-brain barrier model
    • Meister, S. et al. Nanoparticulate flurbiprofen reduces amyloid-β42 generation in an in vitro blood-brain barrier model. Alzheimer's Res. Ther. 5, 51 (2013).
    • (2013) Alzheimer's Res. Ther. , vol.5 , pp. 51
    • Meister, S.1
  • 20
    • 84865603658 scopus 로고    scopus 로고
    • An insight into iTRAQ: Where do we stand now?
    • Evans, C. et al. An insight into iTRAQ: where do we stand now? Anal. Bioanal. Chem. 404, 1011-1027 (2012).
    • (2012) Anal. Bioanal. Chem. , vol.404 , pp. 1011-1027
    • Evans, C.1
  • 21
    • 84865576726 scopus 로고    scopus 로고
    • Quantitative mass spectrometry in proteomics: Critical review update from 2007 to the present
    • Bantscheff, M., Lemeer, S., Savitski, M.M. & Kuster, B. Quantitative mass spectrometry in proteomics: critical review update from 2007 to the present. Anal. Bioanal. Chem. 404, 939-965 (2012).
    • (2012) Anal. Bioanal. Chem. , vol.404 , pp. 939-965
    • Bantscheff, M.1    Lemeer, S.2    Savitski, M.M.3    Kuster, B.4
  • 22
    • 84878011768 scopus 로고    scopus 로고
    • Label-free quantitative proteomics trends for protein-protein interactions
    • Tate, S., Larsen, B., Bonner, R. & Gingras, A.C. Label-free quantitative proteomics trends for protein-protein interactions. J. Proteomics 81, 91-101 (2013).
    • (2013) J. Proteomics , vol.81 , pp. 91-101
    • Tate, S.1    Larsen, B.2    Bonner, R.3    Gingras, A.C.4
  • 23
    • 67650351489 scopus 로고    scopus 로고
    • A comparison of labeling and label-free mass spectrometry-based proteomics approaches
    • Patel, V.J. et al. A comparison of labeling and label-free mass spectrometry-based proteomics approaches. J. Proteome Res. 8, 3752-3759 (2009).
    • (2009) J. Proteome Res. , vol.8 , pp. 3752-3759
    • Patel, V.J.1
  • 24
    • 84879460299 scopus 로고    scopus 로고
    • Characterization of carbon nanotube protein corona by using quantitative proteomics
    • Cai, X. et al. Characterization of carbon nanotube protein corona by using quantitative proteomics. Nanomedicine 9, 583-593 (2013).
    • (2013) Nanomedicine , vol.9 , pp. 583-593
    • Cai, X.1
  • 25
    • 79959499115 scopus 로고    scopus 로고
    • A high-confidence human plasma proteome reference set with estimated concentrations in PeptideAtlas
    • Farrah, T. et al. A high-confidence human plasma proteome reference set with estimated concentrations in PeptideAtlas. Mol. Cell. Proteomics 10, M110.006353 (2011).
    • (2011) Mol. Cell. Proteomics , vol.10
    • Farrah, T.1
  • 27
    • 84907020189 scopus 로고    scopus 로고
    • Simplifying the proteome: Analytical strategies for improving peak capacity
    • Gethings, L.A. & Connolly, J.B. Simplifying the proteome: analytical strategies for improving peak capacity. Adv. Exp. Med. Biol. 806, 59-77 (2014).
    • (2014) Adv. Exp. Med. Biol. , vol.806 , pp. 59-77
    • Gethings, L.A.1    Connolly, J.B.2
  • 28
    • 84862865649 scopus 로고    scopus 로고
    • Impact of the nanoparticle-protein corona on colloidal stability and protein structure
    • Gebauer, J.S. et al. Impact of the nanoparticle-protein corona on colloidal stability and protein structure. Langmuir 28, 9673-9679 (2012).
    • (2012) Langmuir , vol.28 , pp. 9673-9679
    • Gebauer, J.S.1
  • 31
    • 77956215287 scopus 로고    scopus 로고
    • Modeling the time evolution of the nanoparticle-protein corona in a body fluid
    • Dell'Orco, D., Lundqvist, M., Oslakovic, C., Cedervall, T. & Linse, S. Modeling the time evolution of the nanoparticle-protein corona in a body fluid. PLoS ONE 5, e10949 (2010).
    • (2010) PLoS ONE , vol.5
    • Dell'Orco, D.1    Lundqvist, M.2    Oslakovic, C.3    Cedervall, T.4    Linse, S.5
  • 32
    • 84878299053 scopus 로고    scopus 로고
    • Time evolution of nanoparticle-protein corona in human plasma: Relevance for targeted drug delivery
    • Barran-Berdon, A.L. et al. Time evolution of nanoparticle-protein corona in human plasma: relevance for targeted drug delivery. Langmuir 29, 6485-6494 (2013).
    • (2013) Langmuir , vol.29 , pp. 6485-6494
    • Barran-Berdon, A.L.1
  • 33
    • 84872471427 scopus 로고    scopus 로고
    • Impact of polymer shell on the formation and time evolution of nanoparticle-protein corona
    • Natte, K. et al. Impact of polymer shell on the formation and time evolution of nanoparticle-protein corona. Colloids Surf. B Biointerfaces 104, 213-220 (2013).
    • (2013) Colloids Surf. B Biointerfaces , vol.104 , pp. 213-220
    • Natte, K.1
  • 34
    • 70249141572 scopus 로고    scopus 로고
    • A quantitative fluorescence study of protein monolayer formation on colloidal nanoparticles
    • Rocker, C., Potzl, M., Zhang, F., Parak, W.J. & Nienhaus, G.U. A quantitative fluorescence study of protein monolayer formation on colloidal nanoparticles. Nat. Nanotechnol. 4, 577-580 (2009).
    • (2009) Nat. Nanotechnol. , vol.4 , pp. 577-580
    • Rocker, C.1    Potzl, M.2    Zhang, F.3    Parak, W.J.4    Nienhaus, G.U.5
  • 35
    • 80053313445 scopus 로고    scopus 로고
    • The evolution of the protein corona around nanoparticles: A test study
    • Lundqvist, M. et al. The evolution of the protein corona around nanoparticles: a test study. ACS Nano 5, 7503-7509 (2011).
    • (2011) ACS Nano , vol.5 , pp. 7503-7509
    • Lundqvist, M.1
  • 36
    • 28844488494 scopus 로고    scopus 로고
    • Opsonization, biodistribution, and pharmacokinetics of polymeric nanoparticles
    • Owens, D.E. III & Peppas, N.A. Opsonization, biodistribution, and pharmacokinetics of polymeric nanoparticles. Int. J. Pharm. 307, 93-102 (2006).
    • (2006) Int. J. Pharm. , vol.307 , pp. 93-102
    • Owens III, D.E.1    Peppas, N.A.2
  • 37
    • 79952668032 scopus 로고    scopus 로고
    • Irreversible changes in protein conformation due to interaction with superparamagnetic iron oxide nanoparticles
    • Mahmoudi, M. et al. Irreversible changes in protein conformation due to interaction with superparamagnetic iron oxide nanoparticles. Nanoscale 3, 1127-1138 (2011).
    • (2011) Nanoscale , vol.3 , pp. 1127-1138
    • Mahmoudi, M.1
  • 38
    • 56449122424 scopus 로고    scopus 로고
    • The influence of protein adsorption on nanoparticle association with cultured endothelial cells
    • Ehrenberg, M.S., Friedman, A.E., Finkelstein, J.N., Oberdorster, G. & McGrath, J.L. The influence of protein adsorption on nanoparticle association with cultured endothelial cells. Biomaterials 30, 603-610 (2009).
    • (2009) Biomaterials , vol.30 , pp. 603-610
    • Ehrenberg, M.S.1    Friedman, A.E.2    Finkelstein, J.N.3    Oberdorster, G.4    McGrath, J.L.5
  • 39
    • 1842832660 scopus 로고    scopus 로고
    • Influence of surface charge density on protein adsorption on polymeric nanoparticles: Analysis by two-dimensional electrophoresis
    • Gessner, A., Lieske, A., Paulke, B. & Muller, R. Influence of surface charge density on protein adsorption on polymeric nanoparticles: analysis by two-dimensional electrophoresis. Eur. J. Pharm. Biopharm. 54, 165-170 (2002).
    • (2002) Eur. J. Pharm. Biopharm. , vol.54 , pp. 165-170
    • Gessner, A.1    Lieske, A.2    Paulke, B.3    Muller, R.4
  • 40
    • 67349191427 scopus 로고    scopus 로고
    • Interaction of colloidal gold nanoparticles with human blood: Effects on particle size and analysis of plasma protein binding profiles
    • Dobrovolskaia, M.A. et al. Interaction of colloidal gold nanoparticles with human blood: effects on particle size and analysis of plasma protein binding profiles. Nanomedicine (Lond.) 5, 106-117 (2009).
    • (2009) Nanomedicine (Lond.) , vol.5 , pp. 106-117
    • Dobrovolskaia, M.A.1
  • 41
    • 55749091647 scopus 로고    scopus 로고
    • Nanoparticle size and surface properties determine the protein corona with possible implications for biological impacts
    • Lundqvist, M. et al. Nanoparticle size and surface properties determine the protein corona with possible implications for biological impacts. Proc. Natl. Acad. Sci. USA 105, 14265-14270 (2008).
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 14265-14270
    • Lundqvist, M.1
  • 42
    • 79959243546 scopus 로고    scopus 로고
    • Contrasting effect of gold nanoparticles and nanorods with different surface modifications on the structure and activity of bovine serum albumin
    • Chakraborty, S. et al. Contrasting effect of gold nanoparticles and nanorods with different surface modifications on the structure and activity of bovine serum albumin. Langmuir 27, 7722-7731 (2011).
    • (2011) Langmuir , vol.27 , pp. 7722-7731
    • Chakraborty, S.1
  • 43
    • 35448990226 scopus 로고    scopus 로고
    • Adsorbed proteins influence the biological activity and molecular targeting of nanomaterials
    • Dutta, D. et al. Adsorbed proteins influence the biological activity and molecular targeting of nanomaterials. Toxicol. Sci. 100, 303-315 (2007).
    • (2007) Toxicol. Sci. , vol.100 , pp. 303-315
    • Dutta, D.1
  • 44
    • 34547399502 scopus 로고    scopus 로고
    • Detailed identification of plasma proteins adsorbed on copolymer nanoparticles
    • Cedervall, T. et al. Detailed identification of plasma proteins adsorbed on copolymer nanoparticles. Angew Chem. Int. Ed. Engl. 46, 5754-5756 (2007).
    • (2007) Angew Chem. Int. Ed. Engl. , vol.46 , pp. 5754-5756
    • Cedervall, T.1
  • 45
    • 75749123084 scopus 로고    scopus 로고
    • Interaction of gold nanoparticles with common human blood proteins
    • Lacerda, S.H. et al. Interaction of gold nanoparticles with common human blood proteins. ACS Nano 4, 365-379 (2010).
    • (2010) ACS Nano , vol.4 , pp. 365-379
    • Lacerda, S.H.1
  • 46
    • 34248155667 scopus 로고    scopus 로고
    • Systematic investigation of the thermodynamics of HSA adsorption to N-iso-propylacrylamide/N-tert-butylacrylamide copolymer nanoparticles. Effects of particle size and hydrophobicity
    • Lindman, S. et al. Systematic investigation of the thermodynamics of HSA adsorption to N-iso-propylacrylamide/N-tert-butylacrylamide copolymer nanoparticles. Effects of particle size and hydrophobicity. Nano Lett. 7, 914-920 (2007).
    • (2007) Nano Lett. , vol.7 , pp. 914-920
    • Lindman, S.1
  • 47
    • 84883226279 scopus 로고    scopus 로고
    • Temperature: The 'ignored' factor at the NanoBio interface
    • Mahmoudi, M. et al. Temperature: the 'ignored' factor at the NanoBio interface. ACS Nano 7, 6555-6562 (2013).
    • (2013) ACS Nano , vol.7 , pp. 6555-6562
    • Mahmoudi, M.1
  • 48
    • 80053333203 scopus 로고    scopus 로고
    • Toxicity evaluations of superparamagnetic iron oxide nanoparticles: Cell 'vision' versus physicochemical properties of nanoparticles
    • Mahmoudi, M., Laurent, S., Shokrgozar, M.A. & Hosseinkhani, M. Toxicity evaluations of superparamagnetic iron oxide nanoparticles: cell 'vision' versus physicochemical properties of nanoparticles. ACS Nano 5, 7263-7276 (2011).
    • (2011) ACS Nano , vol.5 , pp. 7263-7276
    • Mahmoudi, M.1    Laurent, S.2    Shokrgozar, M.A.3    Hosseinkhani, M.4
  • 49
    • 79952302512 scopus 로고    scopus 로고
    • Physical-chemical aspects of protein corona: Relevance to in vitro and in vivo biological impacts of nanoparticles
    • Monopoli, M.P. et al. Physical-chemical aspects of protein corona: relevance to in vitro and in vivo biological impacts of nanoparticles. J. Am. Chem. Soc. 133, 2525-2534 (2011).
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 2525-2534
    • Monopoli, M.P.1
  • 50
    • 21544437915 scopus 로고    scopus 로고
    • Protein adsorption patterns on poloxamer- and poloxamine-stabilized solid lipid nanoparticles (SLN)
    • Goppert, T.M. & Muller, R.H. Protein adsorption patterns on poloxamer- and poloxamine-stabilized solid lipid nanoparticles (SLN). Eur. J. Pharm. Biopharm. 60, 361-372 (2005).
    • (2005) Eur. J. Pharm. Biopharm. , vol.60 , pp. 361-372
    • Goppert, T.M.1    Muller, R.H.2
  • 51
    • 14844346413 scopus 로고    scopus 로고
    • Interactions of blood proteins with poly(isobutylcyanoac rylate) nanoparticles decorated with a polysaccharidic brush
    • Labarre, D. et al. Interactions of blood proteins with poly(isobutylcyanoac rylate) nanoparticles decorated with a polysaccharidic brush. Biomaterials 26, 5075-5084 (2005).
    • (2005) Biomaterials , vol.26 , pp. 5075-5084
    • Labarre, D.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.