메뉴 건너뛰기




Volumn 357, Issue 1-2, 2010, Pages 17-25

Correlation between the composition of multivalent antibody conjugates with colloidal gold nanoparticles and their affinity

Author keywords

Antibody conjugate; Gold nanoparticle conjugate; Multivalent interaction; Surface plasmon resonance

Indexed keywords

ANTIBODY CONJUGATE; GOLD NANOPARTICLE; IMMUNOGLOBULIN G; COLLOIDAL GOLD; METAL NANOPARTICLE; MONOCLONAL ANTIBODY; VIRUS ANTIBODY;

EID: 77952494421     PISSN: 00221759     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jim.2010.03.010     Document Type: Article
Times cited : (66)

References (46)
  • 1
    • 0033230639 scopus 로고    scopus 로고
    • Surface plasmon resonance (SPR) as a tool for antibody conjugate analysis
    • Adamczyk M., Mattingly P.G., Shreder K., Yu Z. Surface plasmon resonance (SPR) as a tool for antibody conjugate analysis. Bioconjugate Chem. 1999, 10:1032.
    • (1999) Bioconjugate Chem. , vol.10 , pp. 1032
    • Adamczyk, M.1    Mattingly, P.G.2    Shreder, K.3    Yu, Z.4
  • 2
    • 52649165549 scopus 로고    scopus 로고
    • Structure and function of nanoparticle-protein conjugates
    • Aubin-Tam M.E., Hamad-Schifferli K. Structure and function of nanoparticle-protein conjugates. Biomed. Mater. 2008, 3:1.
    • (2008) Biomed. Mater. , vol.3 , pp. 1
    • Aubin-Tam, M.E.1    Hamad-Schifferli, K.2
  • 3
    • 0025733795 scopus 로고
    • Measurement of affinity of viral monoclonal antibodies by ELISA titration of free antibody in equilibrium mixtures
    • Azimzadeh A., Van Regenmortel M.H. Measurement of affinity of viral monoclonal antibodies by ELISA titration of free antibody in equilibrium mixtures. J. Immunol. Meth. 1991, 141:199.
    • (1991) J. Immunol. Meth. , vol.141 , pp. 199
    • Azimzadeh, A.1    Van Regenmortel, M.H.2
  • 5
    • 42149145228 scopus 로고    scopus 로고
    • A simple and convenient approach for evaluation of the parameters of ligand-receptor interaction. Receptor blocking index and its application
    • Bobrovnik S.A. A simple and convenient approach for evaluation of the parameters of ligand-receptor interaction. Receptor blocking index and its application. J. Mol. Recognit. 2008, 21:96.
    • (2008) J. Mol. Recognit. , vol.21 , pp. 96
    • Bobrovnik, S.A.1
  • 8
    • 1542374062 scopus 로고    scopus 로고
    • Valency of antibody binding to virions and its determination by surface plasmon resonance
    • Dimmock N.J., Hardy S.A. Valency of antibody binding to virions and its determination by surface plasmon resonance. Rev. Med. Virol. 2004, 14:123.
    • (2004) Rev. Med. Virol. , vol.14 , pp. 123
    • Dimmock, N.J.1    Hardy, S.A.2
  • 10
    • 0003051583 scopus 로고
    • Controlled nucleation for the regulation of the particle size in monodiperse gold suspensions
    • Frens G. Controlled nucleation for the regulation of the particle size in monodiperse gold suspensions. Nat. Phys. Sci. 1973, 241:20.
    • (1973) Nat. Phys. Sci. , vol.241 , pp. 20
    • Frens, G.1
  • 11
    • 0021964141 scopus 로고
    • Measurements of the true affinity constant in solution of antigen-antibody complexes by enzyme-linked immunosorbent assay
    • Friguet B., Chaffotte A.F., Djavadi-Ohaniance L., Goldberg M.E. Measurements of the true affinity constant in solution of antigen-antibody complexes by enzyme-linked immunosorbent assay. J. Immunol. Meth. 1985, 77:305.
    • (1985) J. Immunol. Meth. , vol.77 , pp. 305
    • Friguet, B.1    Chaffotte, A.F.2    Djavadi-Ohaniance, L.3    Goldberg, M.E.4
  • 14
    • 0026057934 scopus 로고
    • An electrophoretic method for selection of conditions for production of electrophoretically uniform protein colloidal gold complexes
    • Geoghegan W.D. An electrophoretic method for selection of conditions for production of electrophoretically uniform protein colloidal gold complexes. J. Histochem. Cytochem. 1991, 39:111.
    • (1991) J. Histochem. Cytochem. , vol.39 , pp. 111
    • Geoghegan, W.D.1
  • 15
    • 0017717846 scopus 로고
    • Adsorption of horseradish peroxidase, ovomucoid and anti-immunoglobulin to colloidal gold for the indirect detection of concanavalin A, wheat germ agglutinin and goat antihuman immunoglobulin on cell surfaces at the electron microscopic level: a new method, theory and application
    • Geoghegan W.D., Ackerman G.A. Adsorption of horseradish peroxidase, ovomucoid and anti-immunoglobulin to colloidal gold for the indirect detection of concanavalin A, wheat germ agglutinin and goat antihuman immunoglobulin on cell surfaces at the electron microscopic level: a new method, theory and application. J. Histochem. Cytochem. 1977, 25:l187.
    • (1977) J. Histochem. Cytochem. , vol.25
    • Geoghegan, W.D.1    Ackerman, G.A.2
  • 16
    • 0018830428 scopus 로고
    • Passive gold agglutination. An alternative to passive hemagglutination
    • Geoghegan W.D., Ambegaonkar S., Calvanico N.J. Passive gold agglutination. An alternative to passive hemagglutination. J. Immunol. Meth. 1980, 34:11.
    • (1980) J. Immunol. Meth. , vol.34 , pp. 11
    • Geoghegan, W.D.1    Ambegaonkar, S.2    Calvanico, N.J.3
  • 18
    • 0031013908 scopus 로고    scopus 로고
    • Measurement of antibody/antigen association rate constants in solution by a method based on the enzyme-linked immunosorbent assay
    • Hardy F., Djavadi-Ohaniance L., Goldberg M.E. Measurement of antibody/antigen association rate constants in solution by a method based on the enzyme-linked immunosorbent assay. J. Immunol. Meth. 1997, 200:155.
    • (1997) J. Immunol. Meth. , vol.200 , pp. 155
    • Hardy, F.1    Djavadi-Ohaniance, L.2    Goldberg, M.E.3
  • 19
    • 0032488888 scopus 로고    scopus 로고
    • Crystallographic structure of an intact IgG1 monoclonal antibody
    • Harris L.J., Skaletsky E., McPherson A. Crystallographic structure of an intact IgG1 monoclonal antibody. J. Mol. Biol. 1998, 275:861.
    • (1998) J. Mol. Biol. , vol.275 , pp. 861
    • Harris, L.J.1    Skaletsky, E.2    McPherson, A.3
  • 21
    • 0036842171 scopus 로고    scopus 로고
    • Experimental study and mathematical modeling of the interaction between antibodies and antigens on the surface of liposomes
    • Hendrickson O.D., Zherdev A.V., Kaplun A.P., Dzantiev B.B. Experimental study and mathematical modeling of the interaction between antibodies and antigens on the surface of liposomes. Mol. Immunol. 2002, 39:413.
    • (2002) Mol. Immunol. , vol.39 , pp. 413
    • Hendrickson, O.D.1    Zherdev, A.V.2    Kaplun, A.P.3    Dzantiev, B.B.4
  • 22
    • 0001361370 scopus 로고    scopus 로고
    • Preparation of colloidal-gold-labelled-proteins
    • Academic Press, London
    • Hermanson G.T. Preparation of colloidal-gold-labelled-proteins. Bioconjugate Techniques 1996, 593. Academic Press, London.
    • (1996) Bioconjugate Techniques , pp. 593
    • Hermanson, G.T.1
  • 23
    • 0033002586 scopus 로고    scopus 로고
    • Steric effects on multivalent ligand-receptor binding: exclusion of ligand sites by bound cell surface receptors
    • Hlavacek W.S., Posner R.S., Perelson A.S. Steric effects on multivalent ligand-receptor binding: exclusion of ligand sites by bound cell surface receptors. Biophys. J. 1999, 76:3031.
    • (1999) Biophys. J. , vol.76 , pp. 3031
    • Hlavacek, W.S.1    Posner, R.S.2    Perelson, A.S.3
  • 24
    • 0023187664 scopus 로고
    • Evaluation of equilibrium constants fur antigen-antibody interactions by solid phase immunoassay: the binding of paraquat to its elicited mouse monoclonal antibody
    • Hogg P.J., Jonston S.C., Bowles M.R., Pond S.M., Winzor D.J. Evaluation of equilibrium constants fur antigen-antibody interactions by solid phase immunoassay: the binding of paraquat to its elicited mouse monoclonal antibody. Mol. Immunol. 1987, 24:797.
    • (1987) Mol. Immunol. , vol.24 , pp. 797
    • Hogg, P.J.1    Jonston, S.C.2    Bowles, M.R.3    Pond, S.M.4    Winzor, D.J.5
  • 25
    • 33646228165 scopus 로고    scopus 로고
    • Calculated absorption and scattering properties of gold nanoparticles of different size, shape, and composition: applications in biological imaging and biomedicine
    • Jain P.K., Lee K.S., El-Sayed I.H., El-Sayed M.A. Calculated absorption and scattering properties of gold nanoparticles of different size, shape, and composition: applications in biological imaging and biomedicine. J. Phys. Chem. B 2006, 110:7238.
    • (2006) J. Phys. Chem. B , vol.110 , pp. 7238
    • Jain, P.K.1    Lee, K.S.2    El-Sayed, I.H.3    El-Sayed, M.A.4
  • 26
    • 0029030923 scopus 로고
    • Colloidal gold conjugated monoclonal antibodies, studied in the BIAcore biosensor and in the Nycocard immunoassay format
    • Johne B., Hansen K., Mork E., Holtlund J. Colloidal gold conjugated monoclonal antibodies, studied in the BIAcore biosensor and in the Nycocard immunoassay format. J. Immunol. Meth. 1995, 183:167.
    • (1995) J. Immunol. Meth. , vol.183 , pp. 167
    • Johne, B.1    Hansen, K.2    Mork, E.3    Holtlund, J.4
  • 27
    • 0025094259 scopus 로고
    • Polyvalent interaction of antibodies with bacterial cells
    • Karulin A.Y., Dzantiev B.B. Polyvalent interaction of antibodies with bacterial cells. Mol. Immunol. 1990, 27:965.
    • (1990) Mol. Immunol. , vol.27 , pp. 965
    • Karulin, A.Y.1    Dzantiev, B.B.2
  • 28
    • 70349829328 scopus 로고    scopus 로고
    • Optical properties and biomedical applications of plasmonic nanoparticles
    • Khlebtsov N.G., Dykman L.A. Optical properties and biomedical applications of plasmonic nanoparticles. J. Quant. Spectrosc. Radiat. Trans. 2010, 111:1.
    • (2010) J. Quant. Spectrosc. Radiat. Trans. , vol.111 , pp. 1
    • Khlebtsov, N.G.1    Dykman, L.A.2
  • 29
    • 0016756272 scopus 로고
    • Continuous cultures of fused cells secreting antibody of predefined specificity
    • Kohler G., Milstein C. Continuous cultures of fused cells secreting antibody of predefined specificity. Nature 1975, 256:495.
    • (1975) Nature , vol.256 , pp. 495
    • Kohler, G.1    Milstein, C.2
  • 30
    • 0000624742 scopus 로고
    • Nucleotide sequence of the 3' terminal region of plum pox potyvirus RNA
    • Lain S., Riechmann J.L., Mendez E., Garcia J.A. Nucleotide sequence of the 3' terminal region of plum pox potyvirus RNA. Virus Res. 1988, 10:325.
    • (1988) Virus Res. , vol.10 , pp. 325
    • Lain, S.1    Riechmann, J.L.2    Mendez, E.3    Garcia, J.A.4
  • 31
    • 0028344957 scopus 로고
    • Measurement of the dissociation rate constant of antigen/antibody complexes in solution by enzyme-linked immunosorbent assay
    • Larvor M.P., Djavadi-Ohaniance L., Nall B., Goldberg M.E. Measurement of the dissociation rate constant of antigen/antibody complexes in solution by enzyme-linked immunosorbent assay. J. Immunol. Meth. 1994, 170:167.
    • (1994) J. Immunol. Meth. , vol.170 , pp. 167
    • Larvor, M.P.1    Djavadi-Ohaniance, L.2    Nall, B.3    Goldberg, M.E.4
  • 32
    • 0032514905 scopus 로고    scopus 로고
    • Determination of the affinity and kinetic constants for the interaction between the human virus echovirus 11 and its cellular receptor, CD55
    • Lea S.M., Powe R.M., McKee T., Evans D.J., Brown D., Stuart D.I., van der Merwe P.A. Determination of the affinity and kinetic constants for the interaction between the human virus echovirus 11 and its cellular receptor, CD55. J. Biol. Chem. 1998, 273:30443.
    • (1998) J. Biol. Chem. , vol.273 , pp. 30443
    • Lea, S.M.1    Powe, R.M.2    McKee, T.3    Evans, D.J.4    Brown, D.5    Stuart, D.I.6    van der Merwe, P.A.7
  • 33
    • 43049099281 scopus 로고    scopus 로고
    • Measuring binding kinetics of surface-bound molecules using the surface plasmon resonance technique
    • Li B., Chen J., Long M. Measuring binding kinetics of surface-bound molecules using the surface plasmon resonance technique. Anal. Biochem. 2008, 377:195.
    • (2008) Anal. Biochem. , vol.377 , pp. 195
    • Li, B.1    Chen, J.2    Long, M.3
  • 34
    • 17444391646 scopus 로고    scopus 로고
    • Colloidal Au-enhanced surface plasmon resonance immunosensing
    • Lyon L.A., Musick M.D., Natan M.J. Colloidal Au-enhanced surface plasmon resonance immunosensing. Anal. Chem. 1998, 70:5177.
    • (1998) Anal. Chem. , vol.70 , pp. 5177
    • Lyon, L.A.1    Musick, M.D.2    Natan, M.J.3
  • 35
    • 0028875269 scopus 로고
    • On the validity of "functional affinity" determination for antibodies binding to cell surface antigens or other polyvalent antigens
    • Mattes M.J. On the validity of "functional affinity" determination for antibodies binding to cell surface antigens or other polyvalent antigens. Cancer Res. 1995, 55:5733.
    • (1995) Cancer Res. , vol.55 , pp. 5733
    • Mattes, M.J.1
  • 36
    • 0021687074 scopus 로고
    • Sensitive visualization of antigen-antibody reactions in dot and blot immune overlay assays with immunogold and immunogold/silver staining
    • Moeremans M., Daneels G., van Dijck A., Langanger G., De Mey J. Sensitive visualization of antigen-antibody reactions in dot and blot immune overlay assays with immunogold and immunogold/silver staining. J. Immunol. Meth. 1984, 74:353.
    • (1984) J. Immunol. Meth. , vol.74 , pp. 353
    • Moeremans, M.1    Daneels, G.2    van Dijck, A.3    Langanger, G.4    De Mey, J.5
  • 37
    • 78649905674 scopus 로고    scopus 로고
    • in press. The forthcoming applications of gold nanoparticles in drug and gene delivery systems
    • Pissuwan, D., Niidome, T., Cortie, M.B., in press. The forthcoming applications of gold nanoparticles in drug and gene delivery systems. J. Control. Release. http://doi:10.1016/j.jconrel.2009.12.006.
    • J. Control. Release.
    • Pissuwan, D.1    Niidome, T.2    Cortie, M.B.3
  • 38
    • 0021081680 scopus 로고
    • Optimal conditions for the preparation of Fab and F(ab') fragments from monoclonal IgG of different rat IgG subclasses
    • Rousseaux J., Rousseaux-Prevost R., Bazin H. Optimal conditions for the preparation of Fab and F(ab') fragments from monoclonal IgG of different rat IgG subclasses. J. Immunol. Meth. 1983, 64:141.
    • (1983) J. Immunol. Meth. , vol.64 , pp. 141
    • Rousseaux, J.1    Rousseaux-Prevost, R.2    Bazin, H.3
  • 39
    • 0031180451 scopus 로고    scopus 로고
    • Antibody-antigen binding kinetics. A. Model for multivalency antibodies for large antigen systems
    • Sadana A., Vo-Dinh T. Antibody-antigen binding kinetics. A. Model for multivalency antibodies for large antigen systems. Appl. Biochem. Biotechnol. 1997, 67:1.
    • (1997) Appl. Biochem. Biotechnol. , vol.67 , pp. 1
    • Sadana, A.1    Vo-Dinh, T.2
  • 40
    • 0035872345 scopus 로고    scopus 로고
    • Utilization of kinetically enhanced monovalent binding affinity by immunoassays based on multivalent nanoparticle-antibody bioconjugates
    • Soukka T., Harma H., Paukkunen J., Lovgren T. Utilization of kinetically enhanced monovalent binding affinity by immunoassays based on multivalent nanoparticle-antibody bioconjugates. Anal. Chem. 2001, 73:2254.
    • (2001) Anal. Chem. , vol.73 , pp. 2254
    • Soukka, T.1    Harma, H.2    Paukkunen, J.3    Lovgren, T.4
  • 41
    • 35448951213 scopus 로고    scopus 로고
    • Biosensor-surface plasmon resonance methods for quantitative analysis of biomolecular interactions
    • Tanious F.A., Nguyen B., Wilson W.D. Biosensor-surface plasmon resonance methods for quantitative analysis of biomolecular interactions. Meth. Cell Biol. 2008, 84:53.
    • (2008) Meth. Cell Biol. , vol.84 , pp. 53
    • Tanious, F.A.1    Nguyen, B.2    Wilson, W.D.3
  • 43
    • 0031777344 scopus 로고    scopus 로고
    • Examination of the kinetics of herpes simplex virus glycoprotein D binding to the herpes virus entry mediator, using surface plasmon resonance
    • Willis S.H., Rux A.H., Peng C., Whitbeck J.C., Nicola A.V., Lou H. Examination of the kinetics of herpes simplex virus glycoprotein D binding to the herpes virus entry mediator, using surface plasmon resonance. J. Virol 1998, 72:5937.
    • (1998) J. Virol , vol.72 , pp. 5937
    • Willis, S.H.1    Rux, A.H.2    Peng, C.3    Whitbeck, J.C.4    Nicola, A.V.5    Lou, H.6
  • 45
    • 0037462084 scopus 로고    scopus 로고
    • Investigations of bivalent antibody binding on fluid-supported phospholipid membranes: the effect of hapten density
    • Yang T., Baryshnikova O.K., Mao H., Holden M.A., Cremer P.S. Investigations of bivalent antibody binding on fluid-supported phospholipid membranes: the effect of hapten density. J. Am. Chem. Soc. 2003, 125:4779.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 4779
    • Yang, T.1    Baryshnikova, O.K.2    Mao, H.3    Holden, M.A.4    Cremer, P.S.5
  • 46
    • 0031049949 scopus 로고    scopus 로고
    • Interaction between antibodies and hapten-protein conjugates of different composition: theoretical predictions and experimental data
    • Zherdev A.V., Romanenko O.G., Dzantiev B.B. Interaction between antibodies and hapten-protein conjugates of different composition: theoretical predictions and experimental data. J. Immunoassay 1997, 18:67.
    • (1997) J. Immunoassay , vol.18 , pp. 67
    • Zherdev, A.V.1    Romanenko, O.G.2    Dzantiev, B.B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.