메뉴 건너뛰기




Volumn 16, Issue 2, 2014, Pages

Mechanistic aspects of protein corona formation: Insulin adsorption onto gold nanoparticle surfaces

Author keywords

Disulfide bonds; Gold nanoparticles; Health effects; Insulin; Nanobiotechnology; Protein corona; Protein structure; Surface enhanced Raman scattering (SERS)

Indexed keywords


EID: 84892707271     PISSN: 13880764     EISSN: 1572896X     Source Type: Journal    
DOI: 10.1007/s11051-014-2254-0     Document Type: Article
Times cited : (16)

References (96)
  • 2
    • 65749117793 scopus 로고    scopus 로고
    • Nanoparticle interaction with plasma proteins as it relates to particle biodistribution, biocompatibility and therapeutic efficacy
    • 10.1016/j.addr.2009.03.009
    • Aggarwal P, Hall JB, McLeland CB, Dobrovolskaia MA, McNeil SE (2009) Nanoparticle interaction with plasma proteins as it relates to particle biodistribution, biocompatibility and therapeutic efficacy. Adv Drug Deliv Rev 61(6):428-437
    • (2009) Adv Drug Deliv Rev , vol.61 , Issue.6 , pp. 428-437
    • Aggarwal, P.1    Hall, J.B.2    McLeland, C.B.3    Dobrovolskaia, M.A.4    McNeil, S.E.5
  • 3
    • 40149091023 scopus 로고    scopus 로고
    • A single-molecule assay to directly identify solvent-accessible disulfide bonds and probe their effect on protein folding
    • 10.1021/ja077851s
    • Ainavarapu SRK, Wiita AP, Huang HH, Fernandez JM (2007) A single-molecule assay to directly identify solvent-accessible disulfide bonds and probe their effect on protein folding. J Am Chem Soc 130(2):436-437
    • (2007) J Am Chem Soc , vol.130 , Issue.2 , pp. 436-437
    • Ainavarapu, S.R.K.1    Wiita, A.P.2    Huang, H.H.3    Fernandez, J.M.4
  • 4
    • 29844434629 scopus 로고    scopus 로고
    • Gold nanoparticle-cytochrome c complexes: The effect of nanoparticle ligand charge on protein structure
    • 10.1021/la052102e
    • Aubin-Tam M-E, Hamad-Schifferli K (2005) Gold nanoparticle-cytochrome c complexes: the effect of nanoparticle ligand charge on protein structure. Langmuir 21:12080-12084
    • (2005) Langmuir , vol.21 , pp. 12080-12084
    • Aubin-Tam, M.-E.1    Hamad-Schifferli, K.2
  • 5
    • 52649165549 scopus 로고    scopus 로고
    • Structure and function of nanoparticle-protein conjugates
    • 10.1088/1748-6041/3/3/034001
    • Aubin-Tam ME, Hamad-Schifferli K (2008) Structure and function of nanoparticle-protein conjugates. Biomed Mater 3:1-17
    • (2008) Biomed Mater , vol.3 , pp. 1-17
    • Aubin-Tam, M.E.1    Hamad-Schifferli, K.2
  • 6
  • 7
    • 77956308605 scopus 로고    scopus 로고
    • Oxygen activation on gold nanoparticles: Separating the influence of particle size, particle shape and support interaction
    • 10.1039/c002280b
    • Boronat M, Corma A (2010) Oxygen activation on gold nanoparticles: separating the influence of particle size, particle shape and support interaction. Dalton Transact 39(36):8538-8546
    • (2010) Dalton Transact , vol.39 , Issue.36 , pp. 8538-8546
    • Boronat, M.1    Corma, A.2
  • 8
    • 0028510546 scopus 로고
    • Influence of the electric potential of the interface on the adsorption of proteins
    • 10.1016/0927-7765(93)01109-5
    • Bos MA, Shervani Z, Anusiem ACI, Giesbers M, Norde W, Kleijn JM (1994) Influence of the electric potential of the interface on the adsorption of proteins. Colloids Surf B 3(1-2):91-100
    • (1994) Colloids Surf B , vol.3 , Issue.1-2 , pp. 91-100
    • Bos, M.A.1    Shervani, Z.2    Anusiem, A.C.I.3    Giesbers, M.4    Norde, W.5    Kleijn, J.M.6
  • 9
    • 33646774999 scopus 로고    scopus 로고
    • Adsorption-induced conformational changes of proteins onto ceramic particles: Differential scanning calorimetry and FTIR analysis
    • 10.1016/j.jcis.2006.01.065
    • Brandes N, Welzel PB, Werner C, Kroh LW (2006) Adsorption-induced conformational changes of proteins onto ceramic particles: differential scanning calorimetry and FTIR analysis. J Colloid Interface Sci 299:56-69
    • (2006) J Colloid Interface Sci , vol.299 , pp. 56-69
    • Brandes, N.1    Welzel, P.B.2    Werner, C.3    Kroh, L.W.4
  • 10
    • 33847789142 scopus 로고    scopus 로고
    • Understanding the nanoparticle-protein corona using methods to quantify exchange rates and affinities of proteins for nanoparticles
    • 10.1073/pnas.0608582104
    • Cedervall T, Lynch I, Lindman S, Berggård T, Thulin E, Nilsson H, Dawson KA, Linse S (2007) Understanding the nanoparticle-protein corona using methods to quantify exchange rates and affinities of proteins for nanoparticles. Proc Natl Acad Sci USA 104(7):2050-2055
    • (2007) Proc Natl Acad Sci USA , vol.104 , Issue.7 , pp. 2050-2055
    • Cedervall, T.1    Lynch, I.2    Lindman, S.3    Berggård, T.4    Thulin, E.5    Nilsson, H.6    Dawson, K.A.7    Linse, S.8
  • 11
    • 80052763358 scopus 로고    scopus 로고
    • Insulin-coated gold nanoparticles: A plasmonic device for studying metal-protein interactions
    • 10.1002/smll.201100735
    • Chanana M, Correa-Duarte MA, Liz-Marzán LM (2011) Insulin-coated gold nanoparticles: a plasmonic device for studying metal-protein interactions. Small 7(18):2650-2660
    • (2011) Small , vol.7 , Issue.18 , pp. 2650-2660
    • Chanana, M.1    Correa-Duarte, M.A.2    Liz-Marzán, L.M.3
  • 12
    • 84988214162 scopus 로고
    • Surface-enhanced Raman spectroscopy of biomolecules. Part I. -water-soluble proteins, dipeptides and amino acids
    • 10.1002/jrs.1250210109
    • Chumanov GD, Efremov RG, Nabiev IR (1990) Surface-enhanced Raman spectroscopy of biomolecules. Part I. -water-soluble proteins, dipeptides and amino acids. J Raman Spectrosc 21(1):43-48
    • (1990) J Raman Spectrosc , vol.21 , Issue.1 , pp. 43-48
    • Chumanov, G.D.1    Efremov, R.G.2    Nabiev, I.R.3
  • 13
    • 34547481020 scopus 로고    scopus 로고
    • Nanoparticles as catalysts for protein fibrillation
    • 10.1073/pnas.0703194104
    • Colvin VL, Kulinowski KM (2007) Nanoparticles as catalysts for protein fibrillation. Proc Natl Acad Sci USA 104(21):8679-8680
    • (2007) Proc Natl Acad Sci USA , vol.104 , Issue.21 , pp. 8679-8680
    • Colvin, V.L.1    Kulinowski, K.M.2
  • 14
    • 33845373693 scopus 로고
    • Distance dependence of surface-enhanced resonance Raman enhancement in Langmuir-Blodgett dye multilayers
    • 10.1021/j100281a003
    • Cotton TM, Uphaus RA, Mobius D (1986) Distance dependence of surface-enhanced resonance Raman enhancement in Langmuir-Blodgett dye multilayers. J Phys Chem 90(23):6071-6073
    • (1986) J Phys Chem , vol.90 , Issue.23 , pp. 6071-6073
    • Cotton, T.M.1    Uphaus, R.A.2    Mobius, D.3
  • 15
    • 84988201513 scopus 로고
    • Application of surface-enhanced Raman spectroscopy to biological systems
    • 10.1002/jrs.1250221203
    • Cotton TM, Kim J-H, Chumanov GD (1991) Application of surface-enhanced Raman spectroscopy to biological systems. J Raman Spectrosc 22:729-742
    • (1991) J Raman Spectrosc , vol.22 , pp. 729-742
    • Cotton, T.M.1    Kim, J.-H.2    Chumanov, G.D.3
  • 16
    • 0000539428 scopus 로고
    • The problem of how and why proteins adopt folded conformations
    • 10.1021/j100258a006
    • Creighton TE (1985) The problem of how and why proteins adopt folded conformations. J Phys Chem 89(12):2452-2459
    • (1985) J Phys Chem , vol.89 , Issue.12 , pp. 2452-2459
    • Creighton, T.E.1
  • 17
    • 33745285736 scopus 로고    scopus 로고
    • The component polypeptide chains of bovine insulin nucleate or inhibit aggregation of the parent protein in a conformation-dependent manner
    • 10.1016/j.jmb.2006.05.007
    • Devlin GL, Knowles TPJ, Squires A, McCammon MG, Gras SL, Nilsson MR, Robinson CV, Dobson CM, MacPhee CE (2006) The component polypeptide chains of bovine insulin nucleate or inhibit aggregation of the parent protein in a conformation-dependent manner. J Mol Biol 360(2):497-509
    • (2006) J Mol Biol , vol.360 , Issue.2 , pp. 497-509
    • Devlin, G.L.1    Knowles, T.P.J.2    Squires, A.3    McCammon, M.G.4    Gras, S.L.5    Nilsson, M.R.6    Robinson, C.V.7    Dobson, C.M.8    Macphee, C.E.9
  • 18
    • 0038461955 scopus 로고    scopus 로고
    • Insulin assembly damps conformational fluctuations: Raman analysis of amide i linewidths in native states and fibrils
    • 10.1016/S0022-2836(03)00536-9
    • Dong J, Wan Z, Popov M, Carey PR, Weiss MA (2003) Insulin assembly damps conformational fluctuations: Raman analysis of amide I linewidths in native states and fibrils. J Mol Biol 330(2):431-442
    • (2003) J Mol Biol , vol.330 , Issue.2 , pp. 431-442
    • Dong, J.1    Wan, Z.2    Popov, M.3    Carey, P.R.4    Weiss, M.A.5
  • 19
    • 84861389565 scopus 로고    scopus 로고
    • Disulfide bonding in protein biophysics
    • 10.1146/annurev-biophys-050511-102321
    • Fass D (2012) Disulfide bonding in protein biophysics. Annu Rev Biophys 41(1):63-79
    • (2012) Annu Rev Biophys , vol.41 , Issue.1 , pp. 63-79
    • Fass, D.1
  • 22
    • 80051473874 scopus 로고    scopus 로고
    • Bioreducible insulin-loaded nanoparticles and their interaction with model lipid membranes
    • 10.1016/j.jcis.2011.05.082
    • Frost R, Coué G, Engbersen JFJ, Zäch M, Kasemo B, Svedhem S (2011) Bioreducible insulin-loaded nanoparticles and their interaction with model lipid membranes. J Colloid Interf Sci 362(2):575-583
    • (2011) J Colloid Interf Sci , vol.362 , Issue.2 , pp. 575-583
    • Frost, R.1    Coué, G.2    Engbersen, J.F.J.3    Zäch, M.4    Kasemo, B.5    Svedhem, S.6
  • 23
    • 79960846411 scopus 로고    scopus 로고
    • Effect of gold nanoparticle morphology on adsorbed protein structure and function
    • 10.1016/j.biomaterials.2011.05.091
    • Gagner JE, Lopez MD, Dordick JS, Siegel RW (2011) Effect of gold nanoparticle morphology on adsorbed protein structure and function. Biomaterials 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
  • 24
    • 0026189760 scopus 로고
    • Probing biomolecule-surface interactions with surface-enhanced Raman spectroscopy
    • 10.1177/088391159100600308
    • Garrell RL (1991) Probing biomolecule-surface interactions with surface-enhanced Raman spectroscopy. J Bioact Compat Polym 6(3):296-307
    • (1991) J Bioact Compat Polym , vol.6 , Issue.3 , pp. 296-307
    • Garrell, R.L.1
  • 26
    • 78650682753 scopus 로고    scopus 로고
    • Influence of individual ionic components on the agglomeration kinetics of silver nanoparticles
    • 10.1016/j.jcis.2010.11.016
    • Gebauer JS, Treuel L (2011) Influence of individual ionic components on the agglomeration kinetics of silver nanoparticles. J Colloid Interface Sci 354(2):546-554
    • (2011) J Colloid Interface Sci , vol.354 , Issue.2 , pp. 546-554
    • Gebauer, J.S.1    Treuel, L.2
  • 30
    • 77951609685 scopus 로고    scopus 로고
    • Disulfide bond cleavage: A redox reaction without electron transfer
    • 10.1002/chem.200902831
    • Hofbauer F, Frank I (2010) Disulfide bond cleavage: a redox reaction without electron transfer. Chem Eur J 16(17):5097-5101
    • (2010) Chem Eur J , vol.16 , Issue.17 , pp. 5097-5101
    • Hofbauer, F.1    Frank, I.2
  • 31
    • 14044257062 scopus 로고    scopus 로고
    • Effect of colloidal gold size on the conformational changes of adsorbed cytochrome c: Probing by circular dichroism, UV-Vis, and infrared spectroscopy
    • 10.1021/bm049744l
    • Jiang X, Jiang J, Jin Y, Wang E, Dong S (2005) Effect of colloidal gold size on the conformational changes of adsorbed cytochrome c: probing by circular dichroism, UV-Vis, and infrared spectroscopy. Biomacromolecules 6:46-53
    • (2005) Biomacromolecules , vol.6 , pp. 46-53
    • Jiang, X.1    Jiang, J.2    Jin, Y.3    Wang, E.4    Dong, S.5
  • 32
    • 77950140732 scopus 로고    scopus 로고
    • Quantitative analysis of the protein corona on FePt nanoparticles formed by transferrin binding
    • 10.1098/rsif.2009.0272.focus
    • Jiang X, Weise S, Hafner M, Röcker C, Zhang F, Parak WJ, Nienhaus GU (2010) Quantitative analysis of the protein corona on FePt nanoparticles formed by transferrin binding. J R Soc Interface 7(Suppl 1):S5-S13
    • (2010) J R Soc Interface , vol.7 , Issue.SUPPL.1
    • Jiang, X.1    Weise, S.2    Hafner, M.3    Röcker, C.4    Zhang, F.5    Parak, W.J.6    Nienhaus, G.U.7
  • 33
    • 30344469072 scopus 로고    scopus 로고
    • Gold nanoparticles as carriers for efficient transmucosal insulin delivery
    • 10.1021/la051982u
    • Joshi HM, Bhumkar DR, Joshi K, Pokharkar V, Sastry M (2006) Gold nanoparticles as carriers for efficient transmucosal insulin delivery. Langmuir 22(1):300-305
    • (2006) Langmuir , vol.22 , Issue.1 , pp. 300-305
    • Joshi, H.M.1    Bhumkar, D.R.2    Joshi, K.3    Pokharkar, V.4    Sastry, M.5
  • 34
    • 0042582104 scopus 로고    scopus 로고
    • Determination of the distance dependence and experimental effects for modified SERS substrates based on self-assembled monolayers formed using alkanethiols
    • 10.1021/jp984454i
    • Kennedy BJ, Spaeth S, Dickey M, Carron KT (1999) Determination of the distance dependence and experimental effects for modified SERS substrates based on self-assembled monolayers formed using alkanethiols. J Phys Chem B 103(18):3640-3646
    • (1999) J Phys Chem B , vol.103 , Issue.18 , pp. 3640-3646
    • Kennedy, B.J.1    Spaeth, S.2    Dickey, M.3    Carron, K.T.4
  • 35
    • 0019070134 scopus 로고
    • Surface enhanced Raman scattering (SERS) by molecules adsorbed at spherical particles
    • 10.1364/AO.19.003373
    • Kerker M, Wang D-S, Chew H (1980) Surface enhanced Raman scattering (SERS) by molecules adsorbed at spherical particles. Appl Opt 19(19):3373-3388
    • (1980) Appl Opt , vol.19 , Issue.19 , pp. 3373-3388
    • Kerker, M.1    Wang, D.-S.2    Chew, H.3
  • 36
    • 0003007623 scopus 로고    scopus 로고
    • Raman Spectroscopy of Proteins
    • Wiley, New York. doi: 10.1002/0470027320.s8202
    • Kitagawa T, Hirota S (2006) Raman Spectroscopy of Proteins. In: Handbook of vibrational spectroscopy. Wiley, New York. doi: 10.1002/0470027320.s8202
    • (2006) Handbook of Vibrational Spectroscopy
    • Kitagawa, T.1    Hirota, S.2
  • 37
    • 0000221607 scopus 로고
    • The adsorption of proteins from aqueous solution on solid surfaces
    • Kleijn M, Norde W (1995) The adsorption of proteins from aqueous solution on solid surfaces. Heterogeneous Chem Rev 2(3):157-172
    • (1995) Heterogeneous Chem Rev , vol.2 , Issue.3 , pp. 157-172
    • Kleijn, M.1    Norde, W.2
  • 38
    • 33847781099 scopus 로고    scopus 로고
    • Probing the interactions of proteins and nanoparticles
    • 10.1073/pnas.0611610104
    • Klein J (2007) Probing the interactions of proteins and nanoparticles. Proc Natl Acad Sci USA 104(7):2029-2030
    • (2007) Proc Natl Acad Sci USA , vol.104 , Issue.7 , pp. 2029-2030
    • Klein, J.1
  • 39
    • 0022807006 scopus 로고
    • Distance dependence of SERS enhancement factor from Langmuir-Blodgett monolayers on metal island films: Evidence for the electromagnetic mechanism
    • 10.1021/la00072a001
    • Kovacs GJ, Loutfy RO, Vincett PS, Jennings C, Aroca R (1986) Distance dependence of SERS enhancement factor from Langmuir-Blodgett monolayers on metal island films: evidence for the electromagnetic mechanism. Langmuir 2(6):689-694
    • (1986) Langmuir , vol.2 , Issue.6 , pp. 689-694
    • Kovacs, G.J.1    Loutfy, R.O.2    Vincett, P.S.3    Jennings, C.4    Aroca, R.5
  • 40
    • 3242720289 scopus 로고    scopus 로고
    • Dosimetry and toxicology of ultrafine particles
    • 10.1089/0894268041457147
    • Kreyling WG, Semmler M, Möller W (2004) Dosimetry and toxicology of ultrafine particles. J Aerosol Med 17(2):140-152
    • (2004) J Aerosol Med , vol.17 , Issue.2 , pp. 140-152
    • Kreyling, W.G.1    Semmler, M.2    Möller, W.3
  • 41
    • 0023008334 scopus 로고
    • Vibrational spectroscopy and conformation of peptides, polypeptides, and proteins
    • 10.1016/S0065-3233(08)60528-8
    • Krimm S, Bandekar J (1986) Vibrational spectroscopy and conformation of peptides, polypeptides, and proteins. Adv Protein Chem 38:181-364
    • (1986) Adv Protein Chem , vol.38 , pp. 181-364
    • Krimm, S.1    Bandekar, J.2
  • 42
    • 80054045806 scopus 로고    scopus 로고
    • Measuring protein structure and stability of protein-nanoparticle systems with synchrotron radiation circular dichroism
    • 10.1021/nl202909s
    • Laera S, Ceccone G, Rossi F, Gilliland D, Hussain R, Siligardi G, Calzolai L (2011) Measuring protein structure and stability of protein-nanoparticle systems with synchrotron radiation circular dichroism. Nano Lett 11:4480-4484
    • (2011) Nano Lett , vol.11 , pp. 4480-4484
    • Laera, S.1    Ceccone, G.2    Rossi, F.3    Gilliland, D.4    Hussain, R.5    Siligardi, G.6    Calzolai, L.7
  • 44
    • 2842588851 scopus 로고
    • Adsorption and surface-enhanced Raman of dyes on silver and gold sols
    • 10.1021/j100214a025
    • Lee PC, Meisel D (1982) Adsorption and surface-enhanced Raman of dyes on silver and gold sols. J Phys Chem 86(17):3391-3395
    • (1982) J Phys Chem , vol.86 , Issue.17 , pp. 3391-3395
    • Lee, P.C.1    Meisel, D.2
  • 46
    • 55749091647 scopus 로고    scopus 로고
    • Nanoparticle size and surface properties determine the protein corona with possible implications for biological impacts
    • 10.1073/pnas.0805135105
    • Lundqvist M, Stigler J, Elia G, Lynch I, Cedervall T, Dawson KA (2008) Nanoparticle size and surface properties determine the protein corona with possible implications for biological impacts. Proc Natl Acad Sci USA 105(38):14265-14270
    • (2008) Proc Natl Acad Sci USA , vol.105 , Issue.38 , pp. 14265-14270
    • Lundqvist, M.1    Stigler, J.2    Elia, G.3    Lynch, I.4    Cedervall, T.5    Dawson, K.A.6
  • 48
    • 80052727425 scopus 로고    scopus 로고
    • Characterization of protein adsorption onto FePt nanoparticles using dual-focus fluorescence correlation spectroscopy
    • 10.3762/bjnano.2.43
    • Maffre P, Nienhaus K, Amin F, Parak WJ, Nienhaus GU (2011) Characterization of protein adsorption onto FePt nanoparticles using dual-focus fluorescence correlation spectroscopy. Beilstein J Nanotechnol 2:374-383
    • (2011) Beilstein J Nanotechnol , vol.2 , pp. 374-383
    • Maffre, P.1    Nienhaus, K.2    Amin, F.3    Parak, W.J.4    Nienhaus, G.U.5
  • 53
    • 20644449754 scopus 로고    scopus 로고
    • Nanotoxicology: An emerging discipline evolving from studies of ultrafine particles
    • 10.1289/ehp.7339
    • Oberdörster G, Oberdörster E, Oberdörster J (2005) Nanotoxicology: an emerging discipline evolving from studies of ultrafine particles. Environ Health Perspect 113(7):823-839
    • (2005) Environ Health Perspect , vol.113 , Issue.7 , pp. 823-839
    • Oberdörster, G.1    Oberdörster, E.2    Oberdörster, J.3
  • 54
    • 8444228141 scopus 로고    scopus 로고
    • Identification of insulin variants using Raman spectroscopy
    • 10.1016/j.ab.2004.06.013
    • Ortiz C, Zhang D, Xie Y, Davisson VJ, Ben-Amotz D (2004) Identification of insulin variants using Raman spectroscopy. Anal Biochem 332(2):245-252
    • (2004) Anal Biochem , vol.332 , Issue.2 , pp. 245-252
    • Ortiz, C.1    Zhang, D.2    Xie, Y.3    Davisson, V.J.4    Ben-Amotz, D.5
  • 55
    • 0000998508 scopus 로고
    • The "adatom model" of surface enhanced Raman scattering (SERS): The present status
    • 10.1016/0039-6028(84)90251-6
    • Otto A, Billmann J, Eickmans J, Ertürk U, Pettenkofer C (1984) The "adatom model" of surface enhanced Raman scattering (SERS): the present status. Surf Sci 138(2-3):319-338
    • (1984) Surf Sci , vol.138 , Issue.2-3 , pp. 319-338
    • Otto, A.1    Billmann, J.2    Eickmans, J.3    Ertürk, U.4    Pettenkofer, C.5
  • 57
    • 70349448536 scopus 로고    scopus 로고
    • Characterization of the kringle fold and identification of a ubiquitous new class of disulfide rotamers
    • 10.1016/j.jsb.2009.06.003
    • Ozhogina OA, Bominaar EL (2009) Characterization of the kringle fold and identification of a ubiquitous new class of disulfide rotamers. J Struct Biol 168(2):223-233
    • (2009) J Struct Biol , vol.168 , Issue.2 , pp. 223-233
    • Ozhogina, O.A.1    Bominaar, E.L.2
  • 58
    • 0034650323 scopus 로고    scopus 로고
    • Spectroscopic methods for analysis of protein secondary structure
    • 10.1006/abio.1999.4320
    • Pelton JT, McLean LR (2000) Spectroscopic methods for analysis of protein secondary structure. Anal Biochem 277(2):167-176
    • (2000) Anal Biochem , vol.277 , Issue.2 , pp. 167-176
    • Pelton, J.T.1    McLean, L.R.2
  • 59
    • 2542445177 scopus 로고    scopus 로고
    • Adsorption and desorption of lysozyme on nano-sized magnetic particles and its conformational changes
    • 10.1016/j.colsurfb.2004.03.010
    • Peng AG, Hidajat K, Uddin MS (2004) Adsorption and desorption of lysozyme on nano-sized magnetic particles and its conformational changes. Colloids Surf B 35(3-4):169-174
    • (2004) Colloids Surf B , vol.35 , Issue.3-4 , pp. 169-174
    • Peng, A.G.1    Hidajat, K.2    Uddin, M.S.3
  • 60
    • 51849142237 scopus 로고    scopus 로고
    • Bridging biomolecules with nanoparticles: Surface-enhanced Raman scattering from colon carcinoma and normal tissue
    • 10.1002/jrs.1907
    • Pînzaru SC, Andronie LM, Domsa I, Cozar O, Astilean S (2008) Bridging biomolecules with nanoparticles: surface-enhanced Raman scattering from colon carcinoma and normal tissue. J Raman Spectrosc 39(3):331-334
    • (2008) J Raman Spectrosc , vol.39 , Issue.3 , pp. 331-334
    • Pînzaru, S.C.1    Andronie, L.M.2    Domsa, I.3    Cozar, O.4    Astilean, S.5
  • 61
    • 0042288190 scopus 로고
    • Conformational alterations of bovine insulin adsorbed on a silver electrode
    • 10.1016/0022-0728(93)80147-A
    • Reipa V, Gaigalas A, Abramowitz S (1993) Conformational alterations of bovine insulin adsorbed on a silver electrode. J Electroanal Chem 348(1-2):413-428
    • (1993) J Electroanal Chem , vol.348 , Issue.1-2 , pp. 413-428
    • Reipa, V.1    Gaigalas, A.2    Abramowitz, S.3
  • 62
    • 33645459798 scopus 로고    scopus 로고
    • Surface tailoring for controlled protein adsorption: Effect of topography at the nanometer scale and chemistry
    • 10.1021/ja056278e
    • Roach P, Farrar D, Perry CC (2006) Surface tailoring for controlled protein adsorption: effect of topography at the nanometer scale and chemistry. J Am Chem Soc 128(12):3939-3945
    • (2006) J Am Chem Soc , vol.128 , Issue.12 , pp. 3939-3945
    • Roach, P.1    Farrar, D.2    Perry, C.C.3
  • 63
    • 70249141572 scopus 로고    scopus 로고
    • A quantitative fluorescence study of protein monolayer formation on colloidal nanoparticles
    • 10.1038/nnano.2009.195
    • Röcker C, Pötzl M, Zhang F, Parak WJ, Nienhaus GU (2009) A quantitative fluoresence study of protein monolayer formation on colloidal nanoparticles. Nat Nanotechnol 4(9):577-580
    • (2009) Nat Nanotechnol , vol.4 , Issue.9 , pp. 577-580
    • Röcker, C.1    Pötzl, M.2    Zhang, F.3    Parak, W.J.4    Nienhaus, G.U.5
  • 64
    • 16444371242 scopus 로고    scopus 로고
    • A three-dimensional cellular model of the human respiratory tract to study the interaction with particles
    • 10.1165/rcmb.2004-0187OC
    • Rothen-Rutishauser B, Kiama S, Gehr P (2005) A three-dimensional cellular model of the human respiratory tract to study the interaction with particles. Am J Respir Cell Mol Biol 32(4):281-289
    • (2005) Am J Respir Cell Mol Biol , vol.32 , Issue.4 , pp. 281-289
    • Rothen-Rutishauser, B.1    Kiama, S.2    Gehr, P.3
  • 65
    • 0034548053 scopus 로고    scopus 로고
    • Low-temperature activation of molecular oxygen by gold clusters: A stoichiometric process correlated to electron affinity
    • 10.1016/S0301-0104(00)00272-X
    • Salisbury BE, Wallace WT, Whetten RL (2000) Low-temperature activation of molecular oxygen by gold clusters: a stoichiometric process correlated to electron affinity. Chem Phys 262:131-141
    • (2000) Chem Phys , vol.262 , pp. 131-141
    • Salisbury, B.E.1    Wallace, W.T.2    Whetten, R.L.3
  • 66
    • 0344004860 scopus 로고    scopus 로고
    • A holistic approach to protein secondary structure characterization using amide i band raman spectroscopy
    • 10.1006/abio.1999.4034
    • Sane SU, Cramer SM, Przybycien TM (1999) A holistic approach to protein secondary structure characterization using amide I band raman spectroscopy. Anal Biochem 269(2):255-272
    • (1999) Anal Biochem , vol.269 , Issue.2 , pp. 255-272
    • Sane, S.U.1    Cramer, S.M.2    Przybycien, T.M.3
  • 67
    • 67650064945 scopus 로고    scopus 로고
    • SERS microscopy: Nanoparticle probes and biomedical applications
    • 10.1002/cphc.200900119
    • Schlücker S (2009) SERS microscopy: nanoparticle probes and biomedical applications. Chem Phys Chem 10(9-10):1344-1354
    • (2009) Chem Phys Chem , vol.10 , Issue.9-10 , pp. 1344-1354
    • Schlücker, S.1
  • 69
    • 33746937812 scopus 로고    scopus 로고
    • Conformational differences in protein disulfide linkages between normal hair and hair from subjects with trichothiodystrophy: A quantitative analysis by Raman microspectroscopy
    • 10.1002/bip.20515
    • Schlücker S, Liang C, Strehle KR, Digiovanna JJ, Kraemer KH, Levin IW (2006) Conformational differences in protein disulfide linkages between normal hair and hair from subjects with trichothiodystrophy: a quantitative analysis by Raman microspectroscopy. Biopolymers 82(6):615-622
    • (2006) Biopolymers , vol.82 , Issue.6 , pp. 615-622
    • Schlücker, S.1    Liang, C.2    Strehle, K.R.3    Digiovanna, J.J.4    Kraemer, K.H.5    Levin, I.W.6
  • 70
    • 84872953468 scopus 로고    scopus 로고
    • Adsorption of dicarboxylic acids onto nano-structured silver surfaces - Surface-enhanced Raman scattering studies of pH-dependent adsorption geometries
    • 10.1002/jrs.4190
    • Schulte JP, Grass S, Treuel L (2012) Adsorption of dicarboxylic acids onto nano-structured silver surfaces - surface-enhanced Raman scattering studies of pH-dependent adsorption geometries. J Raman Spectrosc 44:247-254
    • (2012) J Raman Spectrosc , vol.44 , pp. 247-254
    • Schulte, J.P.1    Grass, S.2    Treuel, L.3
  • 71
    • 33845727430 scopus 로고    scopus 로고
    • Effects of chromophore orientation and molecule conformation on surface-enhanced Raman scattering studied with alkanoic acids and colloidal silver nanoparticles
    • 10.1063/1.2404648
    • Seballos L, Olson TY, Zhang JZ (2006) Effects of chromophore orientation and molecule conformation on surface-enhanced Raman scattering studied with alkanoic acids and colloidal silver nanoparticles. J Chem Phys 125(23):234706
    • (2006) J Chem Phys , vol.125 , Issue.23 , pp. 234706
    • Seballos, L.1    Olson, T.Y.2    Zhang, J.Z.3
  • 72
    • 46549098648 scopus 로고
    • Raman and normal mode studies of the polypeptide chain conformations in crystalline magnesium and calcium poly(l-glutamate)s
    • 10.1016/0584-8539(85)80098-2
    • Sengupta PK, Krimm S (1985) Raman and normal mode studies of the polypeptide chain conformations in crystalline magnesium and calcium poly(l-glutamate)s. Spectrochim Acta, A 41(1-2):205-207
    • (1985) Spectrochim Acta, A , vol.41 , Issue.1-2 , pp. 205-207
    • Sengupta, P.K.1    Krimm, S.2
  • 74
    • 84862867927 scopus 로고    scopus 로고
    • Molecular interaction of proteins and peptides with nanoparticles
    • 10.1021/nn300415x
    • Shemetov AA, Nabiev I, Sukhanova A (2012) Molecular interaction of proteins and peptides with nanoparticles. ACS Nano 6(6):4585-4602
    • (2012) ACS Nano , vol.6 , Issue.6 , pp. 4585-4602
    • Shemetov, A.A.1    Nabiev, I.2    Sukhanova, A.3
  • 79
    • 5244273838 scopus 로고
    • Surface-enhanced Raman spectroscopy of amino acids and nucleotide bases adsorbed on silver
    • 10.1021/ja00276a005
    • Suh JS, Moskovits M (1986) Surface-enhanced Raman spectroscopy of amino acids and nucleotide bases adsorbed on silver. J Am Chem Soc 108(16):4711-4718
    • (1986) J Am Chem Soc , vol.108 , Issue.16 , pp. 4711-4718
    • Suh, J.S.1    Moskovits, M.2
  • 80
    • 0001489979 scopus 로고    scopus 로고
    • Template-engaged replacement reaction: A one-step approach to the large-scale synthesis of metal nanostructures with hollow interiors
    • 10.1021/nl025531v
    • Sun Y, Mayers BT, Xia Y (2002) Template-engaged replacement reaction: a one-step approach to the large-scale synthesis of metal nanostructures with hollow interiors. Nano Lett 2(5):481-485
    • (2002) Nano Lett , vol.2 , Issue.5 , pp. 481-485
    • Sun, Y.1    Mayers, B.T.2    Xia, Y.3
  • 82
    • 84862889496 scopus 로고    scopus 로고
    • Interaction of nanoparticles with proteins- determination of equilibrium constants
    • Weissig V (ed) Springer Verlag, New York (in press)
    • Treuel L, Malissek M (2012) Interaction of nanoparticles with proteins- determination of equilibrium constants. In: Weissig V (ed) Cellular and Sub-cellular Nanotechnology - Methods and Protocols. Springer Verlag, New York (in press)
    • (2012) Cellular and Sub-cellular Nanotechnology - Methods and Protocols
    • Treuel, L.1    Malissek, M.2
  • 83
    • 84864741149 scopus 로고    scopus 로고
    • Toward a molecular understanding of nanoparticle-protein interactions
    • 10.1007/s12551-012-0072-0
    • Treuel L, Nienhaus GU (2012) Toward a molecular understanding of nanoparticle-protein interactions. Biophys Rev 4(2):137-147
    • (2012) Biophys Rev , vol.4 , Issue.2 , pp. 137-147
    • Treuel, L.1    Nienhaus, G.U.2
  • 84
    • 78349240627 scopus 로고    scopus 로고
    • The influence of surface composition of nanoparticles on their interactions with serum albumin
    • 10.1002/cphc.201000174
    • Treuel L, Malissek M, Gebauer JS, Zellner R (2010) The influence of surface composition of nanoparticles on their interactions with serum albumin. Chem Phys Chem 11(14):3093-3099
    • (2010) Chem Phys Chem , vol.11 , Issue.14 , pp. 3093-3099
    • Treuel, L.1    Malissek, M.2    Gebauer, J.S.3    Zellner, R.4
  • 85
    • 84864920957 scopus 로고    scopus 로고
    • Quantifying the influence of polymer coatings on the serum albumin corona formation around silver and gold nanoparticles
    • 10.1007/s11051-012-1102-3
    • Treuel L, Malissek M, Grass S, Diendorf J, Mahl D, Meyer-Zaika W, Epple M (2012) Quantifying the influence of polymer coatings on the serum albumin corona formation around silver and gold nanoparticles. J Nanopart Res 14(9):395-406
    • (2012) J Nanopart Res , vol.14 , Issue.9 , pp. 395-406
    • Treuel, L.1    Malissek, M.2    Grass, S.3    Diendorf, J.4    Mahl, D.5    Meyer-Zaika, W.6    Epple, M.7
  • 86
    • 84881308513 scopus 로고    scopus 로고
    • New views on cellular uptake and trafficking of manufactured nanoparticles
    • 10.1098/rsif.2012.0939
    • Treuel L, Jiang X, Nienhaus GU (2013) New views on cellular uptake and trafficking of manufactured nanoparticles. J R Soc Interface 10(82):1742-5662
    • (2013) J R Soc Interface , vol.10 , Issue.82 , pp. 1742-5662
    • Treuel, L.1    Jiang, X.2    Nienhaus, G.U.3
  • 87
    • 33846402453 scopus 로고    scopus 로고
    • Spreading of proteins and its effect on adsorption and desorption kinetics
    • 10.1016/j.colsurfb.2006.08.017
    • van der Veen M, Stuart MC, Norde W (2007) Spreading of proteins and its effect on adsorption and desorption kinetics. Colloids Surf B 54(2):136-142
    • (2007) Colloids Surf B , vol.54 , Issue.2 , pp. 136-142
    • Van Der Veen, M.1    Stuart, M.C.2    Norde, W.3
  • 90
    • 49349102106 scopus 로고    scopus 로고
    • Aromatic amino acids providing characteristic motifs in the Raman and SERS spectroscopy of peptides
    • 10.1021/jp8025732
    • Wei F, Zhang D, Halas NJ, Hartgerink JD (2008) Aromatic amino acids providing characteristic motifs in the Raman and SERS spectroscopy of peptides. J Phys Chem B 112(30):9158-9164
    • (2008) J Phys Chem B , vol.112 , Issue.30 , pp. 9158-9164
    • Wei, F.1    Zhang, D.2    Halas, N.J.3    Hartgerink, J.D.4
  • 91
    • 33646547262 scopus 로고    scopus 로고
    • Force-dependent chemical kinetics of disulfide bond reduction observed with single-molecule techniques
    • 10.1073/pnas.0511035103
    • Wiita AP, Ainavarapu SRK, Huang HH, Fernandez JM (2006) Force-dependent chemical kinetics of disulfide bond reduction observed with single-molecule techniques. Proc Natl Acad Sci USA 103(19):7222-7227
    • (2006) Proc Natl Acad Sci USA , vol.103 , Issue.19 , pp. 7222-7227
    • Wiita, A.P.1    Ainavarapu, S.R.K.2    Huang, H.H.3    Fernandez, J.M.4
  • 92
    • 33748310797 scopus 로고    scopus 로고
    • Comparison of the abilities of ambient and manufactured nanoparticles to induce cellular toxicity according to an oxidative stress paradigm
    • 10.1021/nl061025k
    • Xia T, Kovochich M, Brant J, Hotze M, Sempf J, Oberley T, Sioutas C, Yeh JI, Wiesner MR, Nel AE (2006) Comparison of the abilities of ambient and manufactured nanoparticles to induce cellular toxicity according to an oxidative stress paradigm. Nano Lett 6(8):1794-1807
    • (2006) Nano Lett , vol.6 , Issue.8 , pp. 1794-1807
    • Xia, T.1    Kovochich, M.2    Brant, J.3    Hotze, M.4    Sempf, J.5    Oberley, T.6    Sioutas, C.7    Yeh, J.I.8    Wiesner, M.R.9    Nel, A.E.10
  • 93
    • 56049106549 scopus 로고    scopus 로고
    • Comparison of the mechanism of toxicity of zinc oxide and cerium oxide nanoparticles based on dissolution and oxidative stress properties
    • 10.1021/nn800511k
    • Xia T, Kovochich M, Liong M, Mädler L, Gilbert B, Shi H, Yeh JI, Zink JI, Nel AE (2008) Comparison of the mechanism of toxicity of zinc oxide and cerium oxide nanoparticles based on dissolution and oxidative stress properties. ACS Nano 2(10):2121-2134
    • (2008) ACS Nano , vol.2 , Issue.10 , pp. 2121-2134
    • Xia, T.1    Kovochich, M.2    Liong, M.3    Mädler, L.4    Gilbert, B.5    Shi, H.6    Yeh, J.I.7    Zink, J.I.8    Nel, A.E.9
  • 94
    • 0015506181 scopus 로고
    • Laser Raman spectroscopy and the conformation of insulin and proinsulin
    • 10.1016/0022-2836(72)90167-2
    • Yu N-T, Liu CS, O'Shea DC (1972) Laser Raman spectroscopy and the conformation of insulin and proinsulin. J Mol Biol 70(1):117-132
    • (1972) J Mol Biol , vol.70 , Issue.1 , pp. 117-132
    • Yu, N.-T.1    Liu, C.S.2    O'Shea, D.C.3
  • 96
    • 0038170826 scopus 로고    scopus 로고
    • Conformational change of protein cytochrome b-562 adsorbed on colloidal gold particles; Absorption band shift
    • 10.1039/A607451K 10.1039/a607451k
    • Zhou HS, Aoki S, Honma I, Hirasawa M, Nagamune T, Komiyama H (1997) Conformational change of protein cytochrome b-562 adsorbed on colloidal gold particles; absorption band shift. Chem Commun 1997:605-606. doi: 10.1039/A607451K
    • (1997) Chem Commun , vol.1997 , pp. 605-606
    • Zhou, H.S.1    Aoki, S.2    Honma, I.3    Hirasawa, M.4    Nagamune, T.5    Komiyama, H.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.