메뉴 건너뛰기




Volumn 118, Issue 51, 2014, Pages 29739-29749

Impact of surface functionalization of AgNPs on binding and conformational change of hemoglobin (Hb) and hemolytic behavior

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BIOCOMPATIBILITY; CONFORMATIONS; DYNAMIC LIGHT SCATTERING; FLUORESCENCE; HEMOGLOBIN; MEDICAL APPLICATIONS; NANOPARTICLES; SILVER NANOPARTICLES;

EID: 84920018939     PISSN: 19327447     EISSN: 19327455     Source Type: Journal    
DOI: 10.1021/jp5075048     Document Type: Article
Times cited : (35)

References (61)
  • 2
    • 84886944905 scopus 로고    scopus 로고
    • Immobilized silver nanoparticles enhance contact killing and show highest efficacy: Elucidation of the mechanism of bactericidal action of silver
    • Agnihotri, S.; Mukherji, S.; Mukherji, S. Immobilized silver nanoparticles enhance contact killing and show highest efficacy: elucidation of the mechanism of bactericidal action of silver Nanoscale 2013, 5, 7328-7340
    • (2013) Nanoscale , vol.5 , pp. 7328-7340
    • Agnihotri, S.1    Mukherji, S.2    Mukherji, S.3
  • 5
    • 39849099525 scopus 로고    scopus 로고
    • Hyperbranched oly(amidoamine) as the stabilizer and reductant to prepare colloid silver nanoparticles in situ and their antibacterial activity
    • Zhang, Y.; Peng, H.; Huang, W.; Zhou, Y.; Zhang, X.; Yan, D. Hyperbranched oly(amidoamine) as the stabilizer and reductant To prepare colloid silver nanoparticles in situ and their antibacterial activity J. Phys.Chem. C 2008, 112, 2330-2336
    • (2008) J. Phys.Chem. C , vol.112 , pp. 2330-2336
    • Zhang, Y.1    Peng, H.2    Huang, W.3    Zhou, Y.4    Zhang, X.5    Yan, D.6
  • 6
    • 84878103207 scopus 로고    scopus 로고
    • Interfacing engineered nanoparticles with biological systems: Anticipating adverse nano-bio interactions
    • Pelaz, B.; Charron, G.; Pfeiffer, C.; Zhao, Y.; de la Fuente, J. M.; Liang, X.-J.; Parak, W. J.; del Pino, P. Interfacing engineered nanoparticles with biological systems: Anticipating adverse nano-bio interactions Small 2013, 9, 1573-1584
    • (2013) Small , vol.9 , pp. 1573-1584
    • Pelaz, B.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 Pino, P.8
  • 9
    • 84900831275 scopus 로고    scopus 로고
    • Prevention of photooxidation of deoxymyoglobin and reduced cytochrome c during enhanced raman measurements: SERRS with thiol-protected Ag nanoparticles and a TERS technique
    • Tanabe, I.; Egashira, M.; Suzuki, T.; Goto, T.; Ozaki, Y. Prevention of photooxidation of deoxymyoglobin and reduced cytochrome c during enhanced raman measurements: SERRS with thiol-protected Ag nanoparticles and a TERS technique J. Phys.Chem. C 2014, 118, 10329-10334
    • (2014) J. Phys.Chem. C , vol.118 , pp. 10329-10334
    • Tanabe, I.1    Egashira, M.2    Suzuki, T.3    Goto, T.4    Ozaki, Y.5
  • 11
    • 80052087725 scopus 로고    scopus 로고
    • Study of silver nanoparticle-haemoglobin interaction and composite formation
    • Mahato, M.; Pal, P.; Tah, B.; Ghosh, M.; Talapatra, G. B. Study of silver nanoparticle-haemoglobin interaction and composite formation Colloids Surf., B 2011, 88, 141-149
    • (2011) Colloids Surf., B , vol.88 , pp. 141-149
    • Mahato, M.1    Pal, P.2    Tah, B.3    Ghosh, M.4    Talapatra, G.B.5
  • 12
    • 80054045806 scopus 로고    scopus 로고
    • Measuring protein structure and stability of protein-nanoparticle systems with synchrotron radiation circular dichroism
    • Laera, S.; Ceccone, G.; Rossi, F.; Gilliland, D.; Hussain, R.; Siligardi, G.; Calzolai, L. Measuring protein structure and stability of protein-nanoparticle systems with synchrotron radiation circular dichroism Nano Lett. 2011, 1, 4480-4484
    • (2011) Nano Lett. , vol.1 , pp. 4480-4484
    • Laera, S.1    Ceccone, G.2    Rossi, F.3    Gilliland, D.4    Hussain, R.5    Siligardi, G.6    Calzolai, L.7
  • 14
    • 4043075579 scopus 로고    scopus 로고
    • Silica nanoparticle size influences the structure and enzymatic activity of adsorbed lysozyme
    • Vertegel, A. A.; Siegel, R. W.; Dordick, J. S. Silica nanoparticle size influences the structure and enzymatic activity of adsorbed lysozyme Langmuir 2004, 20, 6800-6807
    • (2004) Langmuir , vol.20 , pp. 6800-6807
    • Vertegel, A.A.1    Siegel, R.W.2    Dordick, J.S.3
  • 15
    • 77949529810 scopus 로고    scopus 로고
    • Granzyme B cleavage of autoantigens in autoimmunity
    • Darrah, E.; Rosen, A. Granzyme B cleavage of autoantigens in autoimmunity Cell Death Differ. 2010, 17, 624-632
    • (2010) Cell Death Differ. , vol.17 , pp. 624-632
    • Darrah, E.1    Rosen, A.2
  • 17
    • 84865155590 scopus 로고    scopus 로고
    • Interdisciplinary challenges and promising theranostic effects of nanoscience in Alzheimer's disease
    • Laurent, S.; Ejtehadi, M. R.; Rezaei, M.; Kehoe, P. G.; Mahmoudi, M. Interdisciplinary challenges and promising theranostic effects of nanoscience in Alzheimer's disease RSC Adv. 2012, 2, 5008-5033
    • (2012) RSC Adv. , vol.2 , pp. 5008-5033
    • Laurent, S.1    Ejtehadi, M.R.2    Rezaei, M.3    Kehoe, P.G.4    Mahmoudi, M.5
  • 18
    • 84893642253 scopus 로고    scopus 로고
    • Cell-to-cell transmission of pathogenic proteins in neurodegenerative diseases
    • Guo, J. L.; Lee, V. M. Y. Cell-to-cell transmission of pathogenic proteins in neurodegenerative diseases Nat. Med. 2014, 20, 130-138
    • (2014) Nat. Med. , vol.20 , pp. 130-138
    • Guo, J.L.1    Lee, V.M.Y.2
  • 19
  • 20
    • 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.; Baldelli Bombelli, F.; 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    Baldelli Bombelli, F.6    Dawson, K.A.7
  • 21
    • 84889036006 scopus 로고    scopus 로고
    • Nanoparticle-protein interactions: A thermodynamic and kinetic study of the adsorption of bovine serum albumin to gold nanoparticle surfaces
    • Boulos, S. P.; Davis, T. A.; Yang, J. A.; Lohse, S. E.; Alkilany, A. M.; Holland, L. A.; Murphy, C. J. Nanoparticle-protein interactions: A thermodynamic and kinetic study of the adsorption of bovine serum albumin to gold nanoparticle surfaces Langmuir 2013, 29, 14984-14996
    • (2013) Langmuir , vol.29 , pp. 14984-14996
    • Boulos, S.P.1    Davis, T.A.2    Yang, J.A.3    Lohse, S.E.4    Alkilany, A.M.5    Holland, L.A.6    Murphy, C.J.7
  • 22
    • 84885140491 scopus 로고    scopus 로고
    • Magnetic nanoparticles with covalently bound self-assembled protein corona for advanced biomedical applications
    • Venerando, R.; Miotto, G.; Magro, M.; Dallan, M.; Baratella, D.; Bonaiuto, E.; Zboril, R.; Vianello, F. Magnetic nanoparticles with covalently bound self-assembled protein corona for advanced biomedical applications J. Phys.Chem. C 2013, 117, 20320-20331
    • (2013) J. Phys.Chem. C , vol.117 , pp. 20320-20331
    • Venerando, R.1    Miotto, G.2    Magro, M.3    Dallan, M.4    Baratella, D.5    Bonaiuto, E.6    Zboril, R.7    Vianello, F.8
  • 23
    • 84875968263 scopus 로고    scopus 로고
    • Study of wild-type ±-Synuclein binding and orientation on gold nanoparticles
    • Yang, J. A.; Johnson, B. J.; Wu, S.; Woods, W. S.; George, J. M.; Murphy, C. J. Study of wild-type ±-Synuclein binding and orientation on gold nanoparticles Langmuir 2013, 29, 4603-4615
    • (2013) Langmuir , vol.29 , pp. 4603-4615
    • Yang, J.A.1    Johnson, B.J.2    Wu, S.3    Woods, W.S.4    George, J.M.5    Murphy, C.J.6
  • 24
    • 79959808397 scopus 로고    scopus 로고
    • Proteomic characterization of engineered nanomaterial-protein interactions in relation to surface reactivity
    • Sund, J.; Alenius, H.; Vippola, M.; Savolainen, K.; Puustinen, A. Proteomic characterization of engineered nanomaterial-protein interactions in relation to surface reactivity ACS Nano 2011, 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
  • 26
    • 84878740548 scopus 로고    scopus 로고
    • Nano-silica fabricated with silver nanoparticles: Antifouling adsorbent for efficient dye removal, effective water disinfection and biofouling control
    • Das, S. K.; Khan, M. M. R.; Parandhaman, T.; Laffir, F.; Guha, A. K.; Sekaran, G.; Mandal, A. B. Nano-silica fabricated with silver nanoparticles: Antifouling adsorbent for efficient dye removal, effective water disinfection and biofouling control Nanoscale 2013, 5, 5549-5560
    • (2013) Nanoscale , vol.5 , pp. 5549-5560
    • Das, S.K.1    Khan, M.M.R.2    Parandhaman, T.3    Laffir, F.4    Guha, A.K.5    Sekaran, G.6    Mandal, A.B.7
  • 27
    • 84867650550 scopus 로고    scopus 로고
    • Interactions of nanomaterials and biological systems: Implications to personalized nanomedicine
    • Zhang, X.-Q.; Xu, X.; Bertrand, N.; Pridgen, E.; Swami, A.; Farokhzad, O. C. Interactions of nanomaterials and biological systems: Implications to personalized nanomedicine Adv. Drug Deliver. Rev. 2012, 64, 1363-1384
    • (2012) Adv. Drug Deliver. Rev. , vol.64 , pp. 1363-1384
    • Zhang, X.-Q.1    Xu, X.2    Bertrand, N.3    Pridgen, E.4    Swami, A.5    Farokhzad, O.C.6
  • 28
    • 84860249123 scopus 로고    scopus 로고
    • A cyclodextrin host-guest recognition approach to a label-free electrochemical DNA hybridization biosensor
    • Abbaspour, A.; Noori, A. A cyclodextrin host-guest recognition approach to a label-free electrochemical DNA hybridization biosensor Analyst 2012, 137, 1860-1865
    • (2012) Analyst , vol.137 , pp. 1860-1865
    • Abbaspour, A.1    Noori, A.2
  • 29
    • 84878030837 scopus 로고    scopus 로고
    • Self-assembly of Ag nanoparticles using hydroxypropyl cyclodextrin: Synthesis, characterisation and application for the catalytic reduction of p-nitrophenol
    • Devi, L. B.; Mandal, A. B. Self-assembly of Ag nanoparticles using hydroxypropyl cyclodextrin: synthesis, characterisation and application for the catalytic reduction of p-nitrophenol RSC Adv. 2013, 3, 5238-5253
    • (2013) RSC Adv. , vol.3 , pp. 5238-5253
    • Devi, L.B.1    Mandal, A.B.2
  • 30
    • 0034672325 scopus 로고    scopus 로고
    • Estimation of protein secondary structure from circular dichroism spectra: Comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set
    • Sreerama, N.; Woody, R. W. Estimation of protein secondary structure from circular dichroism spectra: Comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set Anal. Biochem. 2000, 287, 252-260
    • (2000) Anal. Biochem. , vol.287 , pp. 252-260
    • Sreerama, N.1    Woody, R.W.2
  • 31
    • 1942424127 scopus 로고    scopus 로고
    • Secondary-structure analysis of proteins by vacuum-ultraviolet circular dichroism spectroscopy
    • Matsuo, K.; Yonehara, R.; Gekko, K. Secondary-structure analysis of proteins by vacuum-ultraviolet circular dichroism spectroscopy J. Biochem. 2004, 135, 405-411
    • (2004) J. Biochem. , vol.135 , pp. 405-411
    • Matsuo, K.1    Yonehara, R.2    Gekko, K.3
  • 32
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding Anal. Biochem. 1976, 72, 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 33
    • 84864598994 scopus 로고    scopus 로고
    • Cationic peptidopolysaccharides show excellent broad-spectrum antimicrobial activities and high selectivity
    • Li, P.; Zhou, C.; Rayatpisheh, S.; Ye, K.; Poon, Y. F.; Hammond, P. T.; Duan, H.; Chan-Park, M. B. Cationic peptidopolysaccharides show excellent broad-spectrum antimicrobial activities and high selectivity Adv. Mater. 2012, 24, 4130-4137
    • (2012) Adv. Mater. , vol.24 , pp. 4130-4137
    • Li, P.1    Zhou, C.2    Rayatpisheh, S.3    Ye, K.4    Poon, Y.F.5    Hammond, P.T.6    Duan, H.7    Chan-Park, M.B.8
  • 34
    • 0030042975 scopus 로고    scopus 로고
    • Electron transfer between electrodes and heme proteins in protein-DNA films
    • Nassar, A.-E. F.; Rusling, J. F.; Nakashima, N. Electron transfer between electrodes and heme proteins in protein-DNA films J. Am. Chem. Soc. 1996, 118, 3043-3044
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 3043-3044
    • Nassar, A.-E.F.1    Rusling, J.F.2    Nakashima, N.3
  • 35
  • 36
    • 77956855874 scopus 로고    scopus 로고
    • A spectroscopic study on the interaction between ferric oxide nanoparticles and human hemoglobin
    • Zolghadri, S.; Saboury, A. A.; Amin, E.; Moosavi-Movahedi, A. A. A spectroscopic study on the interaction between ferric oxide nanoparticles and human hemoglobin J. Iran. Chem. Soc. 2010, 7, S145-S153
    • (2010) J. Iran. Chem. Soc. , vol.7 , pp. 145-S153
    • Zolghadri, S.1    Saboury, A.A.2    Amin, E.3    Moosavi-Movahedi, A.A.4
  • 37
    • 0001514543 scopus 로고
    • Relationships between structural parameters and Raman frequencies for some planar and nonplanar nickel(II) porphyrins
    • Shelnutt, J. A.; Medforth, C. J.; Berber, M. D.; Barkigia, K. M.; Smith, K. M. Relationships between structural parameters and Raman frequencies for some planar and nonplanar nickel(II) porphyrins J. Am. Chem. Soc. 1991, 113, 4077-4087
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 4077-4087
    • Shelnutt, J.A.1    Medforth, C.J.2    Berber, M.D.3    Barkigia, K.M.4    Smith, K.M.5
  • 38
    • 70450104585 scopus 로고    scopus 로고
    • Effective electrochemical method for investigation of hemoglobin unfolding based on the redox property of heme groups at glassy carbon electrodes
    • Li, X.; Zheng, W.; Zhang, L.; Yu, P.; Lin, Y.; Su, L.; Mao, L. Effective electrochemical method for investigation of hemoglobin unfolding based on the redox property of heme groups at glassy carbon electrodes Anal. Chem. 2009, 81, 8557-8563
    • (2009) Anal. Chem. , vol.81 , pp. 8557-8563
    • Li, X.1    Zheng, W.2    Zhang, L.3    Yu, P.4    Lin, Y.5    Su, L.6    Mao, L.7
  • 39
    • 43049134756 scopus 로고    scopus 로고
    • Infrared and circular dichroism spectroscopic characterisation of secondary structure components of a water treatment coagulant protein extracted from moringa oleifera seeds
    • Kwaambwa, H. M.; Maikokera, R. Infrared and circular dichroism spectroscopic characterisation of secondary structure components of a water treatment coagulant protein extracted from moringa oleifera seeds Colloids Surf., B 2008, 64, 118-125
    • (2008) Colloids Surf., B , vol.64 , pp. 118-125
    • Kwaambwa, H.M.1    Maikokera, R.2
  • 41
    • 21344471402 scopus 로고    scopus 로고
    • General, high-affinity approach for the synthesis of fluorophore appended protein nanoparticle assemblies
    • Sandros, M. G.; Gao, D.; Gokdemir, C.; Benson, D. E. General, high-affinity approach for the synthesis of fluorophore appended protein nanoparticle assemblies Chem. Commun. 2005, 2832-2834
    • (2005) Chem. Commun. , pp. 2832-2834
    • Sandros, M.G.1    Gao, D.2    Gokdemir, C.3    Benson, D.E.4
  • 42
    • 34248342939 scopus 로고    scopus 로고
    • Spectroscopic studies on the interaction between human hemoglobin and CdS quantum dots
    • Shen, X.-C.; Liou, X.-Y.; Ye, L.-P.; Liang, H.; Wang, Z.-Y. Spectroscopic studies on the interaction between human hemoglobin and CdS quantum dots J. Colloid Interface Sci. 2007, 311, 400-406
    • (2007) J. Colloid Interface Sci. , vol.311 , pp. 400-406
    • Shen, X.-C.1    Liou, X.-Y.2    Ye, L.-P.3    Liang, H.4    Wang, Z.-Y.5
  • 43
    • 0021888695 scopus 로고
    • The intrinsic tyrosine fluorescence of histone H1. Steady state and fluorescence decay studies reveal heterogeneous emission
    • Libertini, L. J.; Small, E. W. The intrinsic tyrosine fluorescence of histone H1. Steady state and fluorescence decay studies reveal heterogeneous emission Biophys. J. 1985, 47, 765-772
    • (1985) Biophys. J. , vol.47 , pp. 765-772
    • Libertini, L.J.1    Small, E.W.2
  • 45
    • 84859161694 scopus 로고    scopus 로고
    • Hyper-efficient quenching of non-conjugated pendant polymer by silver nanoparticles: A demonstration and versatile mechanistic proposition
    • Ghosh, D.; Chattopadhyay, N. Hyper-efficient quenching of non-conjugated pendant polymer by silver nanoparticles: A demonstration and versatile mechanistic proposition Chem. Phys. Lett. 2012, 532, 52-56
    • (2012) Chem. Phys. Lett. , vol.532 , pp. 52-56
    • Ghosh, D.1    Chattopadhyay, N.2
  • 46
    • 33746896237 scopus 로고    scopus 로고
    • Steady-state fluorescence quenching applications for studying protein structure and dynamics
    • Mátyus, L.; Szollosi, J.; Jenei, A. Steady-state fluorescence quenching applications for studying protein structure and dynamics J. Photochem. Photobiol. B: Biol. 2006, 83, 223-236
    • (2006) J. Photochem. Photobiol. B: Biol. , vol.83 , pp. 223-236
    • Mátyus, L.1    Szollosi, J.2    Jenei, A.3
  • 47
    • 1842426864 scopus 로고
    • Oxygen quenching of fluorescence in solution: An experimental study of the diffusion process
    • Ware, W. R. Oxygen quenching of fluorescence in solution: An experimental study of the diffusion process J. Phys. Chem. 1962, 66, 455-458
    • (1962) J. Phys. Chem. , vol.66 , pp. 455-458
    • Ware, W.R.1
  • 48
    • 58149173934 scopus 로고    scopus 로고
    • Static and dynamic interaction of a naturally occurring photochromic molecule with bovine serum albumin studied by UV-visible absorption and fluorescence spectroscopy
    • Gentili, P. L.; Ortica, F.; Favaro, G. Static and dynamic interaction of a naturally occurring photochromic molecule with bovine serum albumin studied by UV-visible absorption and fluorescence spectroscopy J. Phys.Chem. B 2008, 112, 16793-16801
    • (2008) J. Phys.Chem. B , vol.112 , pp. 16793-16801
    • Gentili, P.L.1    Ortica, F.2    Favaro, G.3
  • 49
    • 20444421544 scopus 로고    scopus 로고
    • Interpretation of protein adsorption: Surface-induced conformational changes
    • Roach, P.; Farrar, D.; Perry, C. C. Interpretation of protein adsorption: Surface-induced conformational changes J. Am. Chem. Soc. 2005, 127, 8168-8173
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 8168-8173
    • Roach, P.1    Farrar, D.2    Perry, C.C.3
  • 51
    • 34548819311 scopus 로고    scopus 로고
    • Using circular dichroism collected as a function of temperature to determine the thermodynamics of protein unfolding and binding interactions
    • Greenfield, N. J. Using circular dichroism collected as a function of temperature to determine the thermodynamics of protein unfolding and binding interactions Nat. Protocols 2007, 1, 2527-2535
    • (2007) Nat. Protocols , vol.1 , pp. 2527-2535
    • Greenfield, N.J.1
  • 53
    • 75849159965 scopus 로고    scopus 로고
    • PH induced structural modulation and interfacial activity of haemoglobin at the air/water interface
    • Mahato, M.; Pal, P.; Kamilya, T.; Sarkar, R.; Talapatra, G. B. pH induced structural modulation and interfacial activity of haemoglobin at the air/water interface J. Phys.Chem. B 2009, 114, 495-502
    • (2009) J. Phys.Chem. B , vol.114 , pp. 495-502
    • Mahato, M.1    Pal, P.2    Kamilya, T.3    Sarkar, R.4    Talapatra, G.B.5
  • 56
    • 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
  • 57
    • 3242775472 scopus 로고    scopus 로고
    • Toxicity of gold nanoparticles functionalized with cationic and anionic side chains
    • Goodman, C. M.; McCusker, C. D.; Yilmaz, T.; Rotello, V. M. Toxicity of gold nanoparticles functionalized with cationic and anionic side chains Bioconjugate. Chem. 2004, 15, 897-900
    • (2004) Bioconjugate. Chem. , vol.15 , pp. 897-900
    • Goodman, C.M.1    McCusker, C.D.2    Yilmaz, T.3    Rotello, V.M.4
  • 58
    • 84866675135 scopus 로고    scopus 로고
    • Development of screening assays for nanoparticle toxicity assessment in human blood: Preliminary studies with charged Au nanoparticles
    • Love, S. A.; Thompson, J. W.; Haynes, C. L. Development of screening assays for nanoparticle toxicity assessment in human blood: Preliminary studies with charged Au nanoparticles Nanomedicine 2012, 7, 1355-1364
    • (2012) Nanomedicine , vol.7 , pp. 1355-1364
    • Love, S.A.1    Thompson, J.W.2    Haynes, C.L.3
  • 59
    • 79951890716 scopus 로고    scopus 로고
    • Interaction of mesoporous silica nanoparticles with human red blood cell membranes: Size and surface effects
    • Zhao, Y.; Sun, X.; Zhang, G.; Trewyn, B. G.; Slowing, I. I.; Lin, V. S. Y. Interaction of mesoporous silica nanoparticles with human red blood cell membranes: Size and surface effects ACS Nano 2011, 5, 1366-1375
    • (2011) ACS Nano , vol.5 , pp. 1366-1375
    • Zhao, Y.1    Sun, X.2    Zhang, G.3    Trewyn, B.G.4    Slowing, I.I.5    Lin, V.S.Y.6
  • 60
    • 60749122689 scopus 로고    scopus 로고
    • Efficacy of simple short-term in vitro assays for predicting the potential of metal oxide nanoparticles to cause pulmonary inflammation
    • Lu, S.; Duffin, R.; Poland, C.; Daly, P.; Murphy, F.; Drost, E.; MacNee, W.; Stone, V.; Donaldson, K. Efficacy of simple short-term in vitro assays for predicting the potential of metal oxide nanoparticles to cause pulmonary inflammation Environ. Health Perspect. 2009, 117, 241-247
    • (2009) Environ. Health Perspect. , vol.117 , pp. 241-247
    • Lu, S.1    Duffin, R.2    Poland, C.3    Daly, P.4    Murphy, F.5    Drost, E.6    MacNee, W.7    Stone, V.8    Donaldson, K.9
  • 61
    • 80052469871 scopus 로고    scopus 로고
    • Physicochemical characterization and in vitro hemolysis evaluation of silver nanoparticles
    • Choi, J.; Reipa, V.; Hitchins, V. M.; Goering, P. L.; Malinauskas, R. A. Physicochemical characterization and in vitro hemolysis evaluation of silver nanoparticles Toxicol. Sci. 2011, 123, 133-143
    • (2011) Toxicol. Sci. , vol.123 , pp. 133-143
    • Choi, J.1    Reipa, V.2    Hitchins, V.M.3    Goering, P.L.4    Malinauskas, R.A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.