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Volumn 3, Issue 4, 2006, Pages 271-282

Determination of binding constant and stoichiometry for antibody-antigen interaction with surface plasmon resonance

Author keywords

Affinity; Antigen binding fragment; Association rate constant; Binding constant; Dissociation constant; Dissociation rate constant; Maximum binding ratio; Monoclonal antibody; Stoichiometry; Surface plasmon resonance; Variable single chain fragment

Indexed keywords


EID: 34248380793     PISSN: 15701646     EISSN: None     Source Type: Journal    
DOI: 10.2174/157016406780655586     Document Type: Review
Times cited : (47)

References (52)
  • 1
    • 24044460404 scopus 로고    scopus 로고
    • Specificity of protein interactions mediated by BRCT domains of the XRCC1 DNA repair protein
    • Beernink, P. T., Hwang, M., Ramirez, M., Murphy, M. B., Doyle, S. A. and Thelen, M. P. (2005) Specificity of protein interactions mediated by BRCT domains of the XRCC1 DNA repair protein. J. Biol. Chem. 280: 30206-13.
    • (2005) J. Biol. Chem , vol.280 , pp. 30206-30213
    • Beernink, P.T.1    Hwang, M.2    Ramirez, M.3    Murphy, M.B.4    Doyle, S.A.5    Thelen, M.P.6
  • 2
    • 0011091839 scopus 로고
    • W.E. Paul Ed, interaction. CRC Press, Boca Raton, FL, pp
    • Berzofsky, J. A. and Berkower, I. J. (1983) in: W.E. Paul (Ed.) Antibodyantigen interaction. CRC Press, Boca Raton, FL., pp. 595-644.
    • (1983) Antibodyantigen , pp. 595-644
    • Berzofsky, J.A.1    Berkower, I.J.2
  • 3
    • 0026781445 scopus 로고
    • The proteinase: Mucus proteinase inhibitor binding stoichiometry
    • Biemann, H. P. and Koshland, D. E. (1994) The proteinase: mucus proteinase inhibitor binding stoichiometry. J. Biol. Chem. 267: 4370-5.
    • (1994) J. Biol. Chem , vol.267 , pp. 4370-4375
    • Biemann, H.P.1    Koshland, D.E.2
  • 5
    • 3042770596 scopus 로고    scopus 로고
    • Antibodytargeted chemotherapy with the calicheamicin conjugate hu3S193-Nacetyl g calicheamicin dimethyl hydrazide targets Lewis and eliminates Lewis-positive human carcinoma cells and xenografts
    • Boghaert, E. R., Sridharan, L., Armellino, D. C., Khandke, K. M., DiJoseph, J. F., Kunz, A., Dougher, M. M., Jiang, F., et al. (2004) Antibodytargeted chemotherapy with the calicheamicin conjugate hu3S193-Nacetyl g calicheamicin dimethyl hydrazide targets Lewis and eliminates Lewis-positive human carcinoma cells and xenografts. Clin. Cancer Res. 10: 4538-49.
    • (2004) Clin. Cancer Res , vol.10 , pp. 4538-4549
    • Boghaert, E.R.1    Sridharan, L.2    Armellino, D.C.3    Khandke, K.M.4    DiJoseph, J.F.5    Kunz, A.6    Dougher, M.M.7    Jiang, F.8
  • 6
    • 1642578938 scopus 로고    scopus 로고
    • Kinetics screening of antibodies from crude hybridoma samples using Biacore
    • Canziani, G. A., Klakamp, S. and Myszka, D. G. (2004) Kinetics screening of antibodies from crude hybridoma samples using Biacore. Anal. Biochem. 325: 301-7.
    • (2004) Anal. Biochem , vol.325 , pp. 301-307
    • Canziani, G.A.1    Klakamp, S.2    Myszka, D.G.3
  • 9
    • 0001781299 scopus 로고
    • Review:Surface plasmon resonance-The technique and its applications to biomaterial processes
    • Davies, J. (1994) Review:Surface plasmon resonance-The technique and its applications to biomaterial processes. Nanobiology 3: 5-16.
    • (1994) Nanobiology , vol.3 , pp. 5-16
    • Davies, J.1
  • 11
    • 1842787056 scopus 로고    scopus 로고
    • Characterizing high-affinity antigen/antibody complexes by kinetic- and equilibriumbased methods
    • Drake, A. W., Myszka, D. G. and Klakamp, S. L. (2004) Characterizing high-affinity antigen/antibody complexes by kinetic- and equilibriumbased methods. Anal. Biochem. 328: 35-43.
    • (2004) Anal. Biochem , vol.328 , pp. 35-43
    • Drake, A.W.1    Myszka, D.G.2    Klakamp, S.L.3
  • 12
    • 21644486795 scopus 로고    scopus 로고
    • Fine tuning of the specificity of an anti-progesterone antibody by first and second sphere residue engineering
    • Dubreuil, O., Bossus, M., Graille, M., Bilous, M., Savatier, A., Jolivet, M., Ménez, A., Stura, E., et al. (2005) Fine tuning of the specificity of an anti-progesterone antibody by first and second sphere residue engineering. J. Biol. Chem. 280: 24880-7.
    • (2005) J. Biol. Chem , vol.280 , pp. 24880-24887
    • Dubreuil, O.1    Bossus, M.2    Graille, M.3    Bilous, M.4    Savatier, A.5    Jolivet, M.6    Ménez, A.7    Stura, E.8
  • 13
    • 0026759532 scopus 로고
    • Stoichiometry of interaction between interferon gamma and its receptor
    • Fountoulakis, M., Zulauf, M., Lustig, A. and Garotta, G. (1992) Stoichiometry of interaction between interferon gamma and its receptor. Eur. J. Biochem. 208: 781-7.
    • (1992) Eur. J. Biochem , vol.208 , pp. 781-787
    • Fountoulakis, M.1    Zulauf, M.2    Lustig, A.3    Garotta, G.4
  • 14
    • 0027198367 scopus 로고
    • Antigen-antibody binding and mass transport by convection and diffusion to a surface: A two-dimensional computer model of binding and dissociation kinetics
    • Glaser, R.W. (1993) Antigen-antibody binding and mass transport by convection and diffusion to a surface: a two-dimensional computer model of binding and dissociation kinetics. Anal. Biochem. 213: 152-61.
    • (1993) Anal. Biochem , vol.213 , pp. 152-161
    • Glaser, R.W.1
  • 15
    • 0025815631 scopus 로고
    • Investigating protein conformation, dynamics and folding with monoclonal antibodies
    • Goldberg, M. (1991) Investigating protein conformation, dynamics and folding with monoclonal antibodies. TIBS 16: 358-62.
    • (1991) TIBS , vol.16 , pp. 358-362
    • Goldberg, M.1
  • 16
    • 0036132656 scopus 로고    scopus 로고
    • Direct kinetic assay of interactions between small peptides and immobilized antibodies using a surface plasmon resonance biosensor
    • Gomes, P. and Andreu, D. (2002) Direct kinetic assay of interactions between small peptides and immobilized antibodies using a surface plasmon resonance biosensor. J. Immunol. Methods 259: 217-30.
    • (2002) J. Immunol. Methods , vol.259 , pp. 217-230
    • Gomes, P.1    Andreu, D.2
  • 17
    • 0037470618 scopus 로고    scopus 로고
    • Bivalent binding of IgA1 to FcaRI suggests a mechanism for cytokine activation of IgA phagocytosis
    • Herr, A. B., White, C. L., Milburn, C., Wu, C. and Bjorkman, P. J. (2003) Bivalent binding of IgA1 to FcaRI suggests a mechanism for cytokine activation of IgA phagocytosis. J. Mol. Biol. 327: 645-57.
    • (2003) J. Mol. Biol , vol.327 , pp. 645-657
    • Herr, A.B.1    White, C.L.2    Milburn, C.3    Wu, C.4    Bjorkman, P.J.5
  • 18
    • 33745727434 scopus 로고    scopus 로고
    • Mono and bivalent binding of scFv and covalent diabody to murine laminin-1 using radioiodinated proteins and SPR measurements: Effects on tissue retention in vivo
    • Huang, B. C., Davern, S. and Kennel, S. J. (2006) Mono and bivalent binding of scFv and covalent diabody to murine laminin-1 using radioiodinated proteins and SPR measurements: effects on tissue retention in vivo. J. Immunol. Methods 313: 149-60.
    • (2006) J. Immunol. Methods , vol.313 , pp. 149-160
    • Huang, B.C.1    Davern, S.2    Kennel, S.J.3
  • 19
    • 25844519777 scopus 로고    scopus 로고
    • Epitope mapping using mRNA display and a unidirectional nested deletion library
    • Ja, W. W., Olsen, B. N. and Roberts, R. W. (2005) Epitope mapping using mRNA display and a unidirectional nested deletion library. Protein Eng. Des. Sel. 18: 309-19.
    • (2005) Protein Eng. Des. Sel , vol.18 , pp. 309-319
    • Ja, W.W.1    Olsen, B.N.2    Roberts, R.W.3
  • 20
    • 33646903696 scopus 로고    scopus 로고
    • Transiently binding antibody fragments against Lewis x and sialyl-Lewis x
    • Johansson, R., Ohlin, M., Jansson, B. and Ohlson, S. (2006) Transiently binding antibody fragments against Lewis x and sialyl-Lewis x. J. Immunol. Methods 312: 20-6.
    • (2006) J. Immunol. Methods , vol.312 , pp. 20-26
    • Johansson, R.1    Ohlin, M.2    Jansson, B.3    Ohlson, S.4
  • 21
    • 0000625786 scopus 로고
    • Real time BIA. A new biosensor based technology for the direct measurement of biomolecular interactions
    • Fundamentals, Technologies and Applications. Ed. Scheller F. and Schmid R. D, pp
    • Jonsson, U. (1992) Real time BIA. A new biosensor based technology for the direct measurement of biomolecular interactions. Biosensors: Fundamentals, Technologies and Applications. Ed. Scheller F. and Schmid R. D., pp. 467-476.
    • (1992) Biosensors , pp. 467-476
    • Jonsson, U.1
  • 24
    • 0036428763 scopus 로고    scopus 로고
    • Development of monoclonal antibodies against creatine kinase MB2
    • Leickt, L., Grubb, A. and Ohlson, S. (2002) Development of monoclonal antibodies against creatine kinase MB2. Scand J. Clin. Lab. Invest. 62: 423-30.
    • (2002) Scand J. Clin. Lab. Invest , vol.62 , pp. 423-430
    • Leickt, L.1    Grubb, A.2    Ohlson, S.3
  • 25
    • 15444373430 scopus 로고    scopus 로고
    • Determination of binding constant of DNA-binding drug to target DNA by surface plasmon resonance biosensor technology
    • Lin, L.-P., Huang, L.-S., Lin, C.-W., Lee, C.-K., Chen, J.-L., Hsu, S.-M. and Lin, S. (2005) Determination of binding constant of DNA-binding drug to target DNA by surface plasmon resonance biosensor technology. Curr. Drug Targets 5: 61-72.
    • (2005) Curr. Drug Targets , vol.5 , pp. 61-72
    • Lin, L.-P.1    Huang, L.-S.2    Lin, C.-W.3    Lee, C.-K.4    Chen, J.-L.5    Hsu, S.-M.6    Lin, S.7
  • 26
    • 12244301558 scopus 로고    scopus 로고
    • Determination of affinities and antigenic epitopes of bovine cardiac troponin I (cTnI) with monoclonal antibodies by surface plasmon resonance biosensor
    • Liu, X., Wei, J., Song, D., Zhang, Z., Zhang, H. and Luo, G. (2003) Determination of affinities and antigenic epitopes of bovine cardiac troponin I (cTnI) with monoclonal antibodies by surface plasmon resonance biosensor. Anal. Biochem. 314: 301-9.
    • (2003) Anal. Biochem , vol.314 , pp. 301-309
    • Liu, X.1    Wei, J.2    Song, D.3    Zhang, Z.4    Zhang, H.5    Luo, G.6
  • 27
    • 0032773036 scopus 로고    scopus 로고
    • Determination of unbound drug concentration and protein-drug binding fraction in plasma
    • Liu, Z., Li, F. and Huang, Y. (1999) Determination of unbound drug concentration and protein-drug binding fraction in plasma. Biomed. Chromatogr. 13: 262-6.
    • (1999) Biomed. Chromatogr , vol.13 , pp. 262-266
    • Liu, Z.1    Li, F.2    Huang, Y.3
  • 28
    • 0037155910 scopus 로고    scopus 로고
    • Activation-induced conformational changes in the I domain region of lymphocyte function-associated antigen 1
    • Ma, Q., Shimaoka, M., Lu, C., Jing, H., Carman, C. V. and Springer, T. A. (2002) Activation-induced conformational changes in the I domain region of lymphocyte function-associated antigen 1. J. Biol. Chem. 277: 10638-41.
    • (2002) J. Biol. Chem , vol.277 , pp. 10638-10641
    • Ma, Q.1    Shimaoka, M.2    Lu, C.3    Jing, H.4    Carman, C.V.5    Springer, T.A.6
  • 29
    • 0002476950 scopus 로고    scopus 로고
    • What is SPR anyway?
    • Markey, F. (1999) What is SPR anyway? BIA. J. 6: 14-7.
    • (1999) BIA. J , vol.6 , pp. 14-17
    • Markey, F.1
  • 30
    • 0345196632 scopus 로고    scopus 로고
    • Screening of compounds interacting with HIV-1 proteinase using optical biosensor technology
    • Markgren, P.-O., Hämäläinen, M. and Danielson, U. (1999) Screening of compounds interacting with HIV-1 proteinase using optical biosensor technology. Anal. Biochem. 265: 340-50.
    • (1999) Anal. Biochem , vol.265 , pp. 340-350
    • Markgren, P.-O.1    Hämäläinen, M.2    Danielson, U.3
  • 33
    • 0032321401 scopus 로고    scopus 로고
    • Kinetic analysis of macromolecular interactions using surface plasmon resonance biosensors
    • Morton, T. A. and Myszka, D. G. (1998) Kinetic analysis of macromolecular interactions using surface plasmon resonance biosensors. Methods Enzymol. 295: 268-94.
    • (1998) Methods Enzymol , vol.295 , pp. 268-294
    • Morton, T.A.1    Myszka, D.G.2
  • 34
    • 0033226378 scopus 로고    scopus 로고
    • Survey of the 1998 optical biosensor literature
    • Myszka, D. G. (1999) Survey of the 1998 optical biosensor literature. J. Mol. Recognit. 12: 390-408.
    • (1999) J. Mol. Recognit , vol.12 , pp. 390-408
    • Myszka, D.G.1
  • 35
    • 0032535149 scopus 로고    scopus 로고
    • Equilibrium analysis of high affinity interactions using BIACORE
    • Myszka, D. G., Jonsen, M. D. and Graves, B. J. (1998) Equilibrium analysis of high affinity interactions using BIACORE. Anal. Biochem. 265: 326-30.
    • (1998) Anal. Biochem , vol.265 , pp. 326-330
    • Myszka, D.G.1    Jonsen, M.D.2    Graves, B.J.3
  • 36
    • 0037092016 scopus 로고    scopus 로고
    • Influence of compound structure on affinity, sequence selectivity, and mode of binding to DNA for unfused aromatic dications related to furamidine
    • Nguyen, B., Tardy, C., Bailly, C., Colson, P., Houssier, C., Kumar, A., Boykin, D. W. and Wilson, W. D. (2002) Influence of compound structure on affinity, sequence selectivity, and mode of binding to DNA for unfused aromatic dications related to furamidine. Biopolymers 63: 281-97.
    • (2002) Biopolymers , vol.63 , pp. 281-297
    • Nguyen, B.1    Tardy, C.2    Bailly, C.3    Colson, P.4    Houssier, C.5    Kumar, A.6    Boykin, D.W.7    Wilson, W.D.8
  • 37
    • 0034947066 scopus 로고    scopus 로고
    • Reevaluation of stoichiometry and affinity/ avidity in interactions between anti-hapten antibodies and mono- or multi-valent antigens
    • Oda, M. and Azuma T. (2000) Reevaluation of stoichiometry and affinity/ avidity in interactions between anti-hapten antibodies and mono- or multi-valent antigens. Mol. Immunol. 37: 1111-22.
    • (2000) Mol. Immunol , vol.37 , pp. 1111-1122
    • Oda, M.1    Azuma, T.2
  • 38
    • 33745127718 scopus 로고    scopus 로고
    • Regional and segmental flexibility of antibodies in interaction with antigens of different size
    • Oda, M., Uchiyama, S., Robinson, C. V., Fukui, K., Kobayashi, Y. and Azuma, T. (2006) Regional and segmental flexibility of antibodies in interaction with antigens of different size. FEBS J. 273: 1476-87.
    • (2006) FEBS J , vol.273 , pp. 1476-1487
    • Oda, M.1    Uchiyama, S.2    Robinson, C.V.3    Fukui, K.4    Kobayashi, Y.5    Azuma, T.6
  • 39
    • 0035880556 scopus 로고    scopus 로고
    • Complexes between monoclonal antibodies and receptor fragments with a common cold virus: Determination of stoichiometry by capillary electrophoresis
    • Okun, V. M., Moser, R., Blaas, D. and Kenndler, E. (2001) Complexes between monoclonal antibodies and receptor fragments with a common cold virus: determination of stoichiometry by capillary electrophoresis. Anal. Chem. 73: 3900-6.
    • (2001) Anal. Chem , vol.73 , pp. 3900-3906
    • Okun, V.M.1    Moser, R.2    Blaas, D.3    Kenndler, E.4
  • 41
    • 18544364796 scopus 로고    scopus 로고
    • Interaction properties of the procollagen C-proteinase enhancer protein shed light on the mechanism of stimulation of BMP-1
    • Ricard-Blum, S., Bernocco, S., Font, B., Moali, C. Eichenberger, D., Farjane, J., Burchardt, E. R., van der Rest, M., et al. (2002) Interaction properties of the procollagen C-proteinase enhancer protein shed light on the mechanism of stimulation of BMP-1. J. Biol. Chem. 277: 33864-9.
    • (2002) J. Biol. Chem , vol.277 , pp. 33864-33869
    • Ricard-Blum, S.1    Bernocco, S.2    Font, B.3    Moali, C.4    Eichenberger, D.5    Farjane, J.6    Burchardt, E.R.7    van der Rest, M.8
  • 42
    • 0033955735 scopus 로고    scopus 로고
    • Advances in surface plasmon resonance biosensor analysis
    • Rich, R. L. and Myszka, D. G. (2000) Advances in surface plasmon resonance biosensor analysis. Curr. Opin. Biotech. 11: 54-61.
    • (2000) Curr. Opin. Biotech , vol.11 , pp. 54-61
    • Rich, R.L.1    Myszka, D.G.2
  • 43
    • 0032456780 scopus 로고    scopus 로고
    • Thermodynamic analysis of protein interactions with biosensor technology
    • Roos, H., Karlsson, R., Nilshans, H. and Persson, A. (1998) Thermodynamic analysis of protein interactions with biosensor technology. J. Mol. Recognit. 11: 204-10.
    • (1998) J. Mol. Recognit , vol.11 , pp. 204-210
    • Roos, H.1    Karlsson, R.2    Nilshans, H.3    Persson, A.4
  • 44
    • 0037059794 scopus 로고    scopus 로고
    • Platelet-derived growth factor-BB abd basic fibroblast growth factor directly interact in vitro with high affinity
    • Russo, K., Ragone, R., Facchiano, A. M., Capogrossi, M. C. and Facchiano, A. (2002) Platelet-derived growth factor-BB abd basic fibroblast growth factor directly interact in vitro with high affinity. J. Biol. Chem. 277: 1284-91.
    • (2002) J. Biol. Chem , vol.277 , pp. 1284-1291
    • Russo, K.1    Ragone, R.2    Facchiano, A.M.3    Capogrossi, M.C.4    Facchiano, A.5
  • 45
    • 0037373997 scopus 로고    scopus 로고
    • Thermodynamic and kinetic aspects of antibody evolution during the immune response to hapten
    • Sagawa, T., Oda, M., Ishimura, M., Furukawa, K. and Azuma, T. (2003) Thermodynamic and kinetic aspects of antibody evolution during the immune response to hapten. Mol. Immunol. 39: 801-8.
    • (2003) Mol. Immunol , vol.39 , pp. 801-808
    • Sagawa, T.1    Oda, M.2    Ishimura, M.3    Furukawa, K.4    Azuma, T.5
  • 46
    • 1842861793 scopus 로고    scopus 로고
    • Humanization of agonistic anti-human 4-1BB monoclonal antibody using a phag-displayed combinatorial library
    • Son, J. H., Lee, U. H., Lee, J. J., Kwon, B., Kwon, B. S. and Park, J. W. (2004) Humanization of agonistic anti-human 4-1BB monoclonal antibody using a phag-displayed combinatorial library. J. Immunol. Methods 286: 187-201.
    • (2004) J. Immunol. Methods , vol.286 , pp. 187-201
    • Son, J.H.1    Lee, U.H.2    Lee, J.J.3    Kwon, B.4    Kwon, B.S.5    Park, J.W.6
  • 48
    • 0348110323 scopus 로고    scopus 로고
    • Segmental flexibility and avidity of IgM in the interaction of polyvalent antigens
    • Tobita, T., Oda, M. and Azuma, T. (2004) Segmental flexibility and avidity of IgM in the interaction of polyvalent antigens. Mol. Immunol. 40: 803-11.
    • (2004) Mol. Immunol , vol.40 , pp. 803-811
    • Tobita, T.1    Oda, M.2    Azuma, T.3
  • 49
    • 0037140958 scopus 로고    scopus 로고
    • Tumor targeting properties of monoclonal antibodies with different affinity for target antigen CD44V6 in nude mice bearing head-and-neck cancer xenografts
    • Verel, I., Heider, K. H., Siegmund, M., Ostermann, E., Patzelt, E., Sproll, M., Snow, G. B., Adolf, G. R., et al. (2002) Tumor targeting properties of monoclonal antibodies with different affinity for target antigen CD44V6 in nude mice bearing head-and-neck cancer xenografts. Int. J. Cancer 99: 396-402.
    • (2002) Int. J. Cancer , vol.99 , pp. 396-402
    • Verel, I.1    Heider, K.H.2    Siegmund, M.3    Ostermann, E.4    Patzelt, E.5    Sproll, M.6    Snow, G.B.7    Adolf, G.R.8
  • 51
    • 26844466218 scopus 로고    scopus 로고
    • Detection of picomolar levels of interleukin-8 in human saliva by SPR
    • Yang, C. Y., Brooks, E., Li, Y., Denny, P., Ho, C. M., Qi, F., Shi, W., Wolinsky, L., et al. (2005) Detection of picomolar levels of interleukin-8 in human saliva by SPR. Lab Chip 5: 1017-23.
    • (2005) Lab Chip , vol.5 , pp. 1017-1023
    • Yang, C.Y.1    Brooks, E.2    Li, Y.3    Denny, P.4    Ho, C.M.5    Qi, F.6    Shi, W.7    Wolinsky, L.8
  • 52
    • 0032780214 scopus 로고    scopus 로고
    • Kinetics of interaction between 3-hydroxyphthaloyl-beta-lactoglobulin and CD4 molecules
    • Zeder-Lutz, G., Neurath, A. R. and Van Regenmortel, M. H. (1999) Kinetics of interaction between 3-hydroxyphthaloyl-beta-lactoglobulin and CD4 molecules. Biologicals 27: 29-34.
    • (1999) Biologicals , vol.27 , pp. 29-34
    • Zeder-Lutz, G.1    Neurath, A.R.2    Van Regenmortel, M.H.3


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