메뉴 건너뛰기




Volumn 8, Issue 8, 2015, Pages 2733-2743

IgG and fibrinogen driven nanoparticle aggregation

Author keywords

aggregation; corona; immunoglobulin; nanoparticles (NPs); protein

Indexed keywords


EID: 84939267321     PISSN: 19980124     EISSN: 19980000     Source Type: Journal    
DOI: 10.1007/s12274-015-0780-4     Document Type: Article
Times cited : (75)

References (34)
  • 1
    • 79959808397 scopus 로고    scopus 로고
    • Proteomic characterization of engineered nanomaterialprotein interactions in relation to surface reactivity
    • Sund, J.; Alenius, H.; Vippola, M.; Savolainen, K.; Puustinen, A. Proteomic characterization of engineered nanomaterialprotein interactions in relation to surface reactivity. ACS Nano2011, 5, 4300–4309.
    • (2011) ACS Nano , vol.5 , pp. 4300-4309
    • Sund, J.1    Alenius, H.2    Vippola, M.3    Savolainen, K.4    Puustinen, A.5
  • 2
    • 78650725684 scopus 로고    scopus 로고
    • Effects of cell culture media on the dynamic formation of protein-nanoparticle complexes and influence on the cellular response
    • Maiorano, G.; Sabella, S.; Sorce, B.; Brunetti, V.; Malvindi, M. A.; Cingolani, R.; Pompa, P. P. Effects of cell culture media on the dynamic formation of protein-nanoparticle complexes and influence on the cellular response. ACS Nano2010, 4, 7481–7491.
    • (2010) ACS Nano , vol.4 , pp. 7481-7491
    • Maiorano, G.1    Sabella, S.2    Sorce, B.3    Brunetti, V.4    Malvindi, M.A.5    Cingolani, R.6    Pompa, P.P.7
  • 3
    • 55749091647 scopus 로고    scopus 로고
    • Nanoparticle size and surface properties determine the protein corona with possible implications for biological impacts
    • Lundqvist, M.; Stigler, J.; Elia, G.; Lynch, I.; Cedervall, T.; Dawson, K. A. Nanoparticle size and surface properties determine the protein corona with possible implications for biological impacts. Proc. Natl. Acad. Sci. USA2008, 105, 14265–14270.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 14265-14270
    • Lundqvist, M.1    Stigler, J.2    Elia, G.3    Lynch, I.4    Cedervall, T.5    Dawson, K.A.6
  • 6
    • 33847789142 scopus 로고    scopus 로고
    • Understanding the nanoparticle-protein corona using methods to quantify exchange rates and affinities of proteins for nanoparticles
    • Cedervall, T.; Lynch, I.; Lindman, S.; Berggard, T.; Thulin, E.; Nilsson, H.; Dawson, K. A.; Linse, S. Understanding the nanoparticle-protein corona using methods to quantify exchange rates and affinities of proteins for nanoparticles. Proc. Natl. Acad. Sci. USA2007, 104, 2050–2055.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 2050-2055
    • Cedervall, T.1    Lynch, I.2    Lindman, S.3    Berggard, T.4    Thulin, E.5    Nilsson, H.6    Dawson, K.A.7    Linse, S.8
  • 8
    • 84856436072 scopus 로고    scopus 로고
    • Nanoparticle size and surface chemistry determine serum protein adsorption and macrophage uptake
    • Walkey, C. D.; Olsen, J. B.; Guo, H.; Emili, A.; Chan, W. C. Nanoparticle size and surface chemistry determine serum protein adsorption and macrophage uptake. J. Am. Chem. Soc.2012, 134, 2139–2147.
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 2139-2147
    • Walkey, C.D.1    Olsen, J.B.2    Guo, H.3    Emili, A.4    Chan, W.C.5
  • 9
    • 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.; Docter, D.; Rosfa, S.; Wlodarski, A.; Kuharev, J.; Rekik, A.; Knauer, S. K.; Bantz, C.; Nawroth, T.; Bier, C.; Sirirattanapan, J. et al. Nanoparticle size is a critical physicochemical determinant of the human blood plasma corona: A comprehensive quantitative proteomic analysis. ACS Nano2011, 5, 7155–7167.
    • (2011) ACS Nano , vol.5 , pp. 7155-7167
    • Tenzer, S.1    Docter, D.2    Rosfa, S.3    Wlodarski, A.4    Kuharev, J.5    Rekik, A.6    Knauer, S.K.7    Bantz, C.8    Nawroth, T.9    Bier, C.10    Sirirattanapan, J.11
  • 10
    • 77956215287 scopus 로고    scopus 로고
    • Modeling the time evolution of the nanoparticleprotein corona in a body fluid
    • Dell’Orco, D.; Lundqvist, M.; Oslakovic, C.; Cedervall, T.; Linse, S. Modeling the time evolution of the nanoparticleprotein corona in a body fluid. PloS One2010, 5, e10949.
    • (2010) PloS One , vol.5 , pp. 10949
    • Dell’Orco, D.1    Lundqvist, M.2    Oslakovic, C.3    Cedervall, T.4    Linse, S.5
  • 12
    • 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.; Walczyk, D.; Campbell, A.; Elia, G.; Lynch, I.; Bombelli, F. B.; Dawson, K. A. Physical-chemical aspects of protein corona: Relevance to in vitro and in vivo biological impacts of nanoparticles. J. Am. Chem. Soc.2011, 133, 2525–2534.
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 2525-2534
    • Monopoli, M.P.1    Walczyk, D.2    Campbell, A.3    Elia, G.4    Lynch, I.5    Bombelli, F.B.6    Dawson, K.A.7
  • 13
    • 62749100589 scopus 로고    scopus 로고
    • Cytochrome C on silica nanoparticles: Influence of nanoparticle size on protein structure, stability, and activity
    • Shang, W.; Nuffer, J. H.; Muniz-Papandrea, V. A.; Colon, W.; Siegel, R. W.; Dordick, J. S. Cytochrome C on silica nanoparticles: Influence of nanoparticle size on protein structure, stability, and activity. Small2009, 5, 470–476.
    • (2009) Small , vol.5 , pp. 470-476
    • Shang, W.1    Nuffer, J.H.2    Muniz-Papandrea, V.A.3    Colon, W.4    Siegel, R.W.5    Dordick, J.S.6
  • 14
    • 34547562693 scopus 로고    scopus 로고
    • Unfolding of ribonuclease A on silica nanoparticle surfaces
    • Shang, W.; Nuffer, J. H.; Dordick, J. S.; Siegel, R. W. Unfolding of ribonuclease A on silica nanoparticle surfaces. Nano Lett.2007, 7, 1991–1995.
    • (2007) Nano Lett. , vol.7 , pp. 1991-1995
    • Shang, W.1    Nuffer, J.H.2    Dordick, J.S.3    Siegel, R.W.4
  • 15
    • 10044277018 scopus 로고    scopus 로고
    • Protein adsorption onto silica nanoparticles: Conformational changes depend on the particles’ curvature and the protein stability
    • Lundqvist, M.; Sethson, I.; Jonsson, B. H. Protein adsorption onto silica nanoparticles: Conformational changes depend on the particles’ curvature and the protein stability. Langmuir2004, 20, 10639–10647.
    • (2004) Langmuir , vol.20 , pp. 10639-10647
    • Lundqvist, M.1    Sethson, I.2    Jonsson, B.H.3
  • 18
    • 14044257062 scopus 로고    scopus 로고
    • Effect of colloidal gold size on the conformational changes of adsorbed cytochrome C: Probing by circular dichroism, UV-visible, and infrared spectroscopy
    • Jiang, X.; Jiang, J. G.; Jin, Y. D.; Wang, E.; Dong, S. J. Effect of colloidal gold size on the conformational changes of adsorbed cytochrome C: Probing by circular dichroism, UV-visible, and infrared spectroscopy. Biomacromolecules2005, 6, 46–53.
    • (2005) Biomacromolecules , vol.6 , pp. 46-53
    • Jiang, X.1    Jiang, J.G.2    Jin, Y.D.3    Wang, E.4    Dong, S.J.5
  • 19
    • 84862586179 scopus 로고    scopus 로고
    • Physicochemical characteristics of protein-NP bioconjugates: The role of particle curvature and solution conditions on human serum albumin conformation and fibrillogenesis inhibition
    • Goy-Lopez, S.; Juarez, J.; Alatorre-Meda, M.; Casals, E.; Puntes, V. F.; Taboada, P.; Mosquera, V. Physicochemical characteristics of protein-NP bioconjugates: The role of particle curvature and solution conditions on human serum albumin conformation and fibrillogenesis inhibition. Langmuir2012, 28, 9113–9126.
    • (2012) Langmuir , vol.28 , pp. 9113-9126
    • Goy-Lopez, S.1    Juarez, J.2    Alatorre-Meda, M.3    Casals, E.4    Puntes, V.F.5    Taboada, P.6    Mosquera, V.7
  • 20
    • 84862525746 scopus 로고    scopus 로고
    • In situ measurement of bovine serum albumin interaction with gold nanospheres
    • Dominguez-Medina, S.; McDonough, S.; Swanglap, P.; Landes, C. F.; Link, S. In situ measurement of bovine serum albumin interaction with gold nanospheres. Langmuir2012, 28, 9131–9139.
    • (2012) Langmuir , vol.28 , pp. 9131-9139
    • Dominguez-Medina, S.1    McDonough, S.2    Swanglap, P.3    Landes, C.F.4    Link, S.5
  • 21
    • 38349117763 scopus 로고    scopus 로고
    • Adsorption behavior of acidic and basic proteins onto citrate-coated Au surfaces correlated to their native fold, stability, and pI
    • Glomm, W. R.; Halskau, Ø.; Hanneseth, A. M.; Volden, S. Adsorption behavior of acidic and basic proteins onto citrate-coated Au surfaces correlated to their native fold, stability, and pI. J. Phys. Chem. B2007, 111, 14329–14345.
    • (2007) J. Phys. Chem. B , vol.111 , pp. 14329-14345
    • Glomm, W.R.1    Halskau, Ø.2    Hanneseth, A.M.3    Volden, S.4
  • 23
    • 80051527693 scopus 로고    scopus 로고
    • SANS and UV-vis spectroscopy studies of resultant structure from lysozyme adsorption on silica nanoparticles
    • Kumar, S.; Aswal, V. K.; Kohlbrecher, J. SANS and UV-vis spectroscopy studies of resultant structure from lysozyme adsorption on silica nanoparticles. Langmuir2011, 27, 10167–10173.
    • (2011) Langmuir , vol.27 , pp. 10167-10173
    • Kumar, S.1    Aswal, V.K.2    Kohlbrecher, J.3
  • 24
    • 79960846411 scopus 로고    scopus 로고
    • Effect of gold nanoparticle morphology on adsorbed protein structure and function
    • Gagner, J. E.; Lopez, M. D.; Dordick, J. S.; Siegel, R. W. Effect of gold nanoparticle morphology on adsorbed protein structure and function. Biomaterials2011, 32, 7241–7252.
    • (2011) Biomaterials , vol.32 , pp. 7241-7252
    • Gagner, J.E.1    Lopez, M.D.2    Dordick, J.S.3    Siegel, R.W.4
  • 25
    • 80051521864 scopus 로고    scopus 로고
    • Aggregation of silica nanoparticles directed by adsorption of lysozyme
    • Bharti, B.; Meissner, J.; Findenegg, G. H. Aggregation of silica nanoparticles directed by adsorption of lysozyme. Langmuir2011, 27, 9823–9833.
    • (2011) Langmuir , vol.27 , pp. 9823-9833
    • Bharti, B.1    Meissner, J.2    Findenegg, G.H.3
  • 26
    • 79952851709 scopus 로고    scopus 로고
    • Particle and nanoparticle interactions with fibrinogen: The importance of aggregation in nanotoxicology
    • Kendall, M.; Ding, P.; Kendall, K. Particle and nanoparticle interactions with fibrinogen: The importance of aggregation in nanotoxicology. Nanotoxicology2011, 5, 55–65.
    • (2011) Nanotoxicology , vol.5 , pp. 55-65
    • Kendall, M.1    Ding, P.2    Kendall, K.3
  • 27
    • 84867783533 scopus 로고    scopus 로고
    • Molecular interaction of poly(acrylic acid) gold nanoparticles with human fibrinogen
    • Deng, Z. J.; Liang, M.; Toth, I.; Monteiro, M. J.; Minchin, R. F. Molecular interaction of poly(acrylic acid) gold nanoparticles with human fibrinogen. ACS Nano2012, 6, 8962–8969.
    • (2012) ACS Nano , vol.6 , pp. 8962-8969
    • Deng, Z.J.1    Liang, M.2    Toth, I.3    Monteiro, M.J.4    Minchin, R.F.5
  • 29
    • 78651266062 scopus 로고    scopus 로고
    • Stabilization of magnetic iron oxide nanoparticles in biological media by fetal bovine serum (FBS)
    • Wiogo, H. T.; Lim, M.; Bulmus, V.; Yun, J.; Amal, R. Stabilization of magnetic iron oxide nanoparticles in biological media by fetal bovine serum (FBS). Langmuir2011, 27, 843–850.
    • (2011) Langmuir , vol.27 , pp. 843-850
    • Wiogo, H.T.1    Lim, M.2    Bulmus, V.3    Yun, J.4    Amal, R.5
  • 30
    • 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. Langmuir2012, 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
  • 31
    • 80655144964 scopus 로고    scopus 로고
    • Stable nanoparticle aggregates/agglomerates of different sizes and the effect of their size on hemolytic cytotoxicity
    • Zook, J. M.; Maccuspie, R. I.; Locascio, L. E.; Halter, M. D.; Elliott, J. T. Stable nanoparticle aggregates/agglomerates of different sizes and the effect of their size on hemolytic cytotoxicity. Nanotoxicology2011, 5, 517–530.
    • (2011) Nanotoxicology , vol.5 , pp. 517-530
    • Zook, J.M.1    Maccuspie, R.I.2    Locascio, L.E.3    Halter, M.D.4    Elliott, J.T.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.