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Volumn 10, Issue 5, 1997, Pages 203-216

Kinetics and energetics of specific intermolecular interactions

Author keywords

Antibodies; Antige ns; Energetics; Entropy; Epitopes; Euthalpy; Kinetics; Paratopes; Thermodynamics

Indexed keywords

ANTIBODY COMBINING SITE; ANTIGEN ANTIBODY REACTION; ANTIGEN STRUCTURE; EPITOPE; PROTEIN PROTEIN INTERACTION;

EID: 0031225123     PISSN: 09523499     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1099-1352(199709/10)10:5<203::AID-JMR366>3.0.CO;2-Z     Document Type: Review
Times cited : (42)

References (67)
  • 1
    • 0022570896 scopus 로고
    • The nature of the antigen bond and the factors affecting its association and dissociation
    • Absolom, D. R. and van Oss, C. J. (1986) The nature of the antigen bond and the factors affecting its association and dissociation. Crit. Rev. Immunol. 6, 1-46.
    • (1986) Crit. Rev. Immunol. , vol.6 , pp. 1-46
    • Absolom, D.R.1    Van Oss, C.J.2
  • 2
    • 0025733795 scopus 로고
    • Measurement of affinity of viral monoclonal antibodies by ELISA titration of free antibody in equilibrium mixtures
    • Azimzadeh, A., and van Regenmortel, M. H. V. (1991). Measurement of affinity of viral monoclonal antibodies by ELISA titration of free antibody in equilibrium mixtures. J. Immunol. Meth. 141, 199-208.
    • (1991) J. Immunol. Meth. , vol.141 , pp. 199-208
    • Azimzadeh, A.1    Van Regenmortel, M.H.V.2
  • 3
    • 0026829635 scopus 로고
    • Operational aspects of antibody affinity constants measured by liquid-phase and solid-phase assays
    • Azimzedeh, A., Pellequer, J. L., and van Regenmortel, M. H. V. (1992). Operational aspects of antibody affinity constants measured by liquid-phase and solid-phase assays. J. Molec. Recognition. 5, 9-18.
    • (1992) J. Molec. Recognition. , vol.5 , pp. 9-18
    • Azimzedeh, A.1    Pellequer, J.L.2    Van Regenmortel, M.H.V.3
  • 5
    • 0029717697 scopus 로고    scopus 로고
    • Comparative interaction kinetics of two recombinant Fabs and of the corresponding antibodies directed to the coat protein of tobacco mosaic virus
    • Chatellier, J., Rauffer-Bruyère, N., van Regenmortel, M. H. V., and Altschuh, D. (1996). Comparative interaction kinetics of two recombinant Fabs and of the corresponding antibodies directed to the coat protein of tobacco mosaic virus. J. Molec. Recognition 9, 39-51.
    • (1996) J. Molec. Recognition , vol.9 , pp. 39-51
    • Chatellier, J.1    Rauffer-Bruyère, N.2    Van Regenmortel, M.H.V.3    Altschuh, D.4
  • 6
    • 0028422442 scopus 로고
    • Surface thermodynamics of ozone-induced particle destabilization
    • Chheda, P. and Grasso, D. (1994). Surface thermodynamics of ozone-induced particle destabilization. Langmuir 10, 1044-1053.
    • (1994) Langmuir , vol.10 , pp. 1044-1053
    • Chheda, P.1    Grasso, D.2
  • 7
    • 0038473199 scopus 로고
    • Impact of ozone on the stability of montmorillionite suspensions
    • Chheda, P., Grasso, D., and van Oss, C. J. (1992). Impact of ozone on the stability of montmorillionite suspensions. J. Colloid Interface Sci. 153, 226-236.
    • (1992) J. Colloid Interface Sci. , vol.153 , pp. 226-236
    • Chheda, P.1    Grasso, D.2    Van Oss, C.J.3
  • 8
    • 0003210996 scopus 로고
    • Kinetics of protein sorption on phospholipid membranes measured by ellipsometry
    • Proteins at Interfaces, ed. by J. L. Brash and T. A. Horbett. American Chemical Society, Washington, D.C.
    • Cuypers, P. A., Willems, G. M., Kop, J. M. M., Corsel, J. W., Janssen, M. P. and Hermens, W. Th. (1987). Kinetics of protein sorption on phospholipid membranes measured by ellipsometry. In Proteins at Interfaces, ed. by J. L. Brash and T. A. Horbett. ACS Symp. Series 343, pp. 208-221. American Chemical Society, Washington, D.C.
    • (1987) ACS Symp. Series , vol.343 , pp. 208-221
    • Cuypers, P.A.1    Willems, G.M.2    Kop, J.M.M.3    Corsel, J.W.4    Janssen, M.P.5    Hermens, W.Th.6
  • 12
    • 0029395478 scopus 로고
    • Win some, lose some: Enthalpy-entropy compensation in weak intermolecular interactions
    • Dunitz, J. D. (1995). Win some, lose some: enthalpy-entropy compensation in weak intermolecular interactions. Chem. Biol. 2, 709-712.
    • (1995) Chem. Biol. , vol.2 , pp. 709-712
    • Dunitz, J.D.1
  • 13
    • 0015311978 scopus 로고
    • The valency of IgM and IgG rabbit anti-dextran antibody as a function of the size of the dextranmolecule
    • Edberg, S. C., Bronson, P. M. and van Oss, C. J. (1972). The valency of IgM and IgG rabbit anti-dextran antibody as a function of the size of the dextranmolecule. Immunochemistry. 9, 273-288.
    • (1972) Immunochemistry , vol.9 , pp. 273-288
    • Edberg, S.C.1    Bronson, P.M.2    Van Oss, C.J.3
  • 14
    • 15244356768 scopus 로고
    • Theoretical observations on the Brownian motion
    • Einstein, A. (1907). Theoretical observations on the Brownian motion. Z. F. Elektrochemie. 13, 41-42; In Einstein, A. (1956). Investigations on the theory of the Brownian movement. pp. 63-67, Dover, New York.
    • (1907) Z. F. Elektrochemie. , vol.13 , pp. 41-42
    • Einstein, A.1
  • 16
    • 0002491214 scopus 로고
    • Biosensor techniques
    • ed. by C. J. van Oss and M. H. V. van Regenmortel, Marcel Dekker, New York
    • Fägerstam, L. G. and Karlsson, R. (1994). Biosensor techniques. In Immunochemistry, ed. by C. J. van Oss and M. H. V. van Regenmortel, pp. 949-970. Marcel Dekker, New York.
    • (1994) Immunochemistry , pp. 949-970
    • Fägerstam, L.G.1    Karlsson, R.2
  • 17
    • 0028309424 scopus 로고
    • Adhesion forces between individual ligand-receptor pairs
    • Florin, E. L., Moy, J. T. and Gaub, H. E. (1994). Adhesion forces between individual ligand-receptor pairs. Science 264, 415-417.
    • (1994) Science , vol.264 , pp. 415-417
    • Florin, E.L.1    Moy, J.T.2    Gaub, H.E.3
  • 18
    • 0021964141 scopus 로고
    • Measurement of the true affinity constant in solutions of antigen-antibody complexes by enzyme-linked immunosorbent assay
    • Friguet, B., Chaffotte, A. F., Djavadi-Ohaniance, L. and Goldberg, M. E. (1985). Measurement of the true affinity constant in solutions of antigen-antibody complexes by enzyme-linked immunosorbent assay. J. immunol. Meth. 77, 305-319.
    • (1985) J. Immunol. Meth. , vol.77 , pp. 305-319
    • Friguet, B.1    Chaffotte, A.F.2    Djavadi-Ohaniance, L.3    Goldberg, M.E.4
  • 19
    • 0029053975 scopus 로고
    • Measurement of kinetic binding constants of a panel of antisaporin antibodies using a resonant mirror biosensor
    • George, A. J. T., French, R. R. and Glennie, M. J. (1995). Measurement of kinetic binding constants of a panel of antisaporin antibodies using a resonant mirror biosensor. J.Immunol. Meth. 183, 51-63.
    • (1995) J.Immunol. Meth. , vol.183 , pp. 51-63
    • George, A.J.T.1    French, R.R.2    Glennie, M.J.3
  • 20
    • 33751157207 scopus 로고
    • Enthalpyentropy compensation in drug-receptor binding
    • Gilli, P., Ferretti, V., Gilli, G., and Borea, P. A. (1994). Enthalpyentropy compensation in drug-receptor binding. J. Phys. Chem. 98, 1515-1518.
    • (1994) J. Phys. Chem. , vol.98 , pp. 1515-1518
    • Gilli, P.1    Ferretti, V.2    Gilli, G.3    Borea, P.A.4
  • 25
    • 0030237630 scopus 로고    scopus 로고
    • Effects of secondary forces on the ligand binding properties and variable domain conformations of a monoclonal anti-fluorescyl antibody
    • Hummert, M. E. and Voss, E. W. (1996). Effects of secondary forces on the ligand binding properties and variable domain conformations of a monoclonal anti-fluorescyl antibody. Molec. Immunol. 33, 1067-1077.
    • (1996) Molec. Immunol. , vol.33 , pp. 1067-1077
    • Hummert, M.E.1    Voss, E.W.2
  • 27
    • 0030052290 scopus 로고    scopus 로고
    • Role of hydration and water structure in biological and colloidal interactions
    • Israelachvili, J. N. and Wennerström, H. (1996). Role of hydration and water structure in biological and colloidal interactions. Nature 319, 219-225.
    • (1996) Nature , vol.319 , pp. 219-225
    • Israelachvili, J.N.1    Wennerström, H.2
  • 28
    • 0027328372 scopus 로고
    • Effects of substitutions of closely related amino acids at the contact surface in an antigen-antibody complex on thermodynamic parameters
    • Ito, W., Iba, Y. and Kurosawa, Y. (1993). Effects of substitutions of closely related amino acids at the contact surface in an antigen-antibody complex on thermodynamic parameters. J. Biol. Chem. 268, 16639-16647.
    • (1993) J. Biol. Chem. , vol.268 , pp. 16639-16647
    • Ito, W.1    Iba, Y.2    Kurosawa, Y.3
  • 30
    • 0026607039 scopus 로고
    • Long-range attraction and molecular rearrangements in receptor-ligand interactions
    • Leckband, D. E., Israelachvili, J. N., Schmitt, F. J. and Knoll, W. (1992). Long-range attraction and molecular rearrangements in receptor-ligand interactions. Science 255, 1419-1421.
    • (1992) Science , vol.255 , pp. 1419-1421
    • Leckband, D.E.1    Israelachvili, J.N.2    Schmitt, F.J.3    Knoll, W.4
  • 31
    • 0028805495 scopus 로고
    • Significant discrepancies between van't Hoff and calorimetric enthalpies. II
    • Liu, Y. and Sturtevant, J. M. (1995). Significant discrepancies between van't Hoff and calorimetric enthalpies. II. Protein Sci. 4, 2559-2561.
    • (1995) Protein Sci. , vol.4 , pp. 2559-2561
    • Liu, Y.1    Sturtevant, J.M.2
  • 32
    • 0002300553 scopus 로고    scopus 로고
    • Hydrogen-bond kinetics in liquid water
    • Luzar, A. and Chandler, D. (1996). Hydrogen-bond kinetics in liquid water. Nature 379, 55-57.
    • (1996) Nature , vol.379 , pp. 55-57
    • Luzar, A.1    Chandler, D.2
  • 33
    • 0027410832 scopus 로고
    • The basics of binding: Mechanisms of antigen recognition and mimicry by antibodies
    • Mariuzza, R. A. and Poljak, R. J. (1993). The basics of binding: mechanisms of antigen recognition and mimicry by antibodies. Current Opin. Immun. 5, 50-55.
    • (1993) Current Opin. Immun. , vol.5 , pp. 50-55
    • Mariuzza, R.A.1    Poljak, R.J.2
  • 34
    • 0028299082 scopus 로고
    • The energetics of antigen-antibody binding
    • Mariuzza, R. A., Poljak, R. J. and Schwarz, F. P. (1994) The energetics of antigen-antibody binding. Res. Immunol. 145, 70-72.
    • (1994) Res. Immunol. , vol.145 , pp. 70-72
    • Mariuzza, R.A.1    Poljak, R.J.2    Schwarz, F.P.3
  • 35
    • 0018821664 scopus 로고
    • Thermodynamics of hapten-antibody interactions
    • Mukkur, T. K. S. (1980) Thermodynamics of hapten-antibody interactions. Trends Biochem. Sci. 5, 72-74.
    • (1980) Trends Biochem. Sci. , vol.5 , pp. 72-74
    • Mukkur, T.K.S.1
  • 36
    • 0021315275 scopus 로고
    • Thermodynamics of hapten-antibody interactions
    • Mukkur, T. K. S. (1984) Thermodynamics of hapten-antibody interactions. Crit. Rev. Biochem. 16, 133-167
    • (1984) Crit. Rev. Biochem. , vol.16 , pp. 133-167
    • Mukkur, T.K.S.1
  • 39
    • 0014319627 scopus 로고
    • Specifically impermeable precipitate membranes formed through double diffusion in gels: Behavior with complex forming and with simple systems
    • van Oss, C. J. (1968). Specifically impermeable precipitate membranes formed through double diffusion in gels: behavior with complex forming and with simple systems. J. Colloid Interface Sci. 27, 684-690.
    • (1968) J. Colloid Interface Sci. , vol.27 , pp. 684-690
    • Van Oss, C.J.1
  • 40
    • 0344204636 scopus 로고
    • Precipitation and Agglutination
    • ed. by N. R. Rose, F. Milgrom and C. J. van Oss, Macmillan, New York
    • van Oss, C. J. (1979). Precipitation and Agglutination. In Principles of Immunology, ed. by N. R. Rose, F. Milgrom and C. J. van Oss, pp. 80-106. Macmillan, New York.
    • (1979) Principles of Immunology , pp. 80-106
    • Van Oss, C.J.1
  • 41
    • 0025443497 scopus 로고
    • Aspecific and specific intermolecular interactions in aqueous media
    • van Oss, C. J. (1990). Aspecific and specific intermolecular interactions in aqueous media. J. Molec. Recognition. 3, 128-136.
    • (1990) J. Molec. Recognition , vol.3 , pp. 128-136
    • Van Oss, C.J.1
  • 42
    • 0003354439 scopus 로고
    • Precipitation and agglutination
    • ed. by M. H. V. van Regenmortel, CRC Press, Boca Raton, FL
    • van Oss, C. J. (1992). Precipitation and agglutination. In Structure of Antigens. Vol 1, ed. by M. H. V. van Regenmortel, pp. 179-208. CRC Press, Boca Raton, FL.
    • (1992) Structure of Antigens , vol.1 , pp. 179-208
    • Van Oss, C.J.1
  • 44
    • 7144230563 scopus 로고
    • Precipitation and agglutination
    • ed. by C. J. van Oss and M. H. V. van Regenmortel, Marcel Dekker, New York
    • van Oss, C. J. (1994b). Precipitation and agglutination. In Immunochemistry. ed. by C. J. van Oss and M. H. V. van Regenmortel, pp. 737-758. Marcel Dekker, New York.
    • (1994) Immunochemistry , pp. 737-758
    • Van Oss, C.J.1
  • 45
    • 0002897028 scopus 로고
    • Nature of specific ligand-receptor bonds, in particular the antigen-antibody bond
    • ed by C. J. van Oss and M. H. V. van Regenmortel, Marcel Dekker, New York
    • van Oss, C. J. (1994c). Nature of specific ligand-receptor bonds, in particular the antigen-antibody bond. In Immunochemistry. ed by C. J. van Oss and M. H. V. van Regenmortel, pp. 581-614. Marcel Dekker, New York.
    • (1994) Immunochemistry , pp. 581-614
    • Van Oss, C.J.1
  • 46
    • 0342692736 scopus 로고
    • Cell Interactions and surface hydrophilicity: Influence of Lewis acid-base and electrostatic forces
    • ed. by J. Bauer, CRC Press, Boca Raton, FL
    • van Oss, C. J. (1994d). Cell Interactions and surface hydrophilicity: influence of Lewis acid-base and electrostatic forces. In Cell Electrophoresis. ed. by J. Bauer, pp. 219-239. CRC Press, Boca Raton, FL.
    • (1994) Cell Electrophoresis , pp. 219-239
    • Van Oss, C.J.1
  • 47
    • 0028935073 scopus 로고
    • Hydrophobie, hydrophilic and other interactions in epitope-paratope binding
    • van Oss, C. J. (1995). Hydrophobie, hydrophilic and other interactions in epitope-paratope binding. J. Molec. Immunol. 32, 199-211.
    • (1995) J. Molec. Immunol. , vol.32 , pp. 199-211
    • Van Oss, C.J.1
  • 48
    • 0029550712 scopus 로고    scopus 로고
    • Hydrophobicity of biosurfaces-Origin, quantitative determination and interaction energies
    • van Oss, C. J. (1996). Hydrophobicity of biosurfaces-Origin, quantitative determination and interaction energies. Colloids Surfaces B: Biointerfaces. 5, 91-110.
    • (1996) Colloids Surfaces B: Biointerfaces , vol.5 , pp. 91-110
    • Van Oss, C.J.1
  • 49
    • 84873769643 scopus 로고
    • Qualitative and quantitative interpretation of double diffusion
    • van Oss, C. J. and Heck, Y. S. L. (1961). Qualitative and quantitative interpretation of double diffusion. Z. Immunitätsforschung. 122, 44-57.
    • (1961) Z. Immunitätsforschung. , vol.122 , pp. 44-57
    • Van Oss, C.J.1    Heck, Y.S.L.2
  • 50
    • 0002989186 scopus 로고
    • Interprétation qualitative et quantitative de la précipitation par double diffusion
    • van Oss, C. J. and Heck, Y. S. L. (1963). Interprétation qualitative et quantitative de la précipitation par double diffusion. Revue d'Immunologic. 27, 27-41.
    • (1963) Revue d'Immunologic. , vol.27 , pp. 27-41
    • Van Oss, C.J.1    Heck, Y.S.L.2
  • 51
    • 0021373935 scopus 로고
    • The "equilibrium distance" between two bodies immersed in a liquid
    • van Oss, C. J. and Good, R. J. (1984). The "equilibrium distance" between two bodies immersed in a liquid. Colloids Surfaces. 8, 373-381.
    • (1984) Colloids Surfaces , vol.8 , pp. 373-381
    • Van Oss, C.J.1    Good, R.J.2
  • 52
    • 0025867659 scopus 로고
    • Surface enthalpy and entropy and the physico-chemical nature of hydrophobic and hydrophilic interactiions
    • van Oss, C. J. and Good, R. J. (1991). Surface enthalpy and entropy and the physico-chemical nature of hydrophobic and hydrophilic interactiions. J. Dispersion Sci. Technol. 12, 273-288.
    • (1991) J. Dispersion Sci. Technol. , vol.12 , pp. 273-288
    • Van Oss, C.J.1    Good, R.J.2
  • 53
    • 0030159360 scopus 로고    scopus 로고
    • Hydrogen bonding, interfacial tension and the aqueous solubility of organic compounds
    • van Oss, C. J. and Good, R. J. (1996). Hydrogen bonding, interfacial tension and the aqueous solubility of organic compounds. J. Dispersion Sci. Technol. 17, 433-449.
    • (1996) J. Dispersion Sci. Technol. , vol.17 , pp. 433-449
    • Van Oss, C.J.1    Good, R.J.2
  • 54
    • 84907108298 scopus 로고
    • Repulsive van der Waals forces. I. Complete dissociation of antigen-antibody complexes by means of negative van der Waals forces
    • van Oss, C. J., Absolom, D. R., Grossberg, A. L. and Neumann, A. W. (1979). Repulsive van der Waals forces. I. Complete dissociation of antigen-antibody complexes by means of negative van der Waals forces. Immunol. Commun. 8, 11-29.
    • (1979) Immunol. Commun. , vol.8 , pp. 11-29
    • Van Oss, C.J.1    Absolom, D.R.2    Grossberg, A.L.3    Neumann, A.W.4
  • 55
    • 0022236912 scopus 로고
    • Inhibition of association vs. dissociation of high-avidity DNA-anti-DNA complexes
    • van Oss, C. J., Smeenk, R. J. T. and Aarden, L. A. (1985). Inhibition of association vs. dissociation of high-avidity DNA-anti-DNA complexes. Immunol. Invest. 14, 245-253.
    • (1985) Immunol. Invest. , vol.14 , pp. 245-253
    • Van Oss, C.J.1    Smeenk, R.J.T.2    Aarden, L.A.3
  • 57
    • 26544476885 scopus 로고
    • Interfacial Lifshitz-van der Waals and polar interactions in macroscopic systems
    • van Oss, C. J., Chaudhury, M. K. and Good, R. J. (1988). Interfacial Lifshitz-van der Waals and polar interactions in macroscopic systems. Chem. Rev. 88, 927-941.
    • (1988) Chem. Rev. , vol.88 , pp. 927-941
    • Van Oss, C.J.1    Chaudhury, M.K.2    Good, R.J.3
  • 61
    • 0018385243 scopus 로고
    • Determination of avidity of anti-viral antibodies at 50% binding of antibody
    • van Reqeumortel, M. H. V. and Hardie, G. (1979). Determination of avidity of anti-viral antibodies at 50% binding of antibody. J. Immunol Methods, 27, 43-54.
    • (1979) J. Immunol Methods , vol.27 , pp. 43-54
    • Van Reqeumortel, M.H.V.1    Hardie, G.2
  • 62
    • 0019889063 scopus 로고
    • Thermodynamics of protein association reactions: Forces contributing to stability
    • Ross, P. D. and Subramanian, S. (1981). Thermodynamics of protein association reactions: forces contributing to stability. Biochemistry 20, 3096-3102.
    • (1981) Biochemistry , vol.20 , pp. 3096-3102
    • Ross, P.D.1    Subramanian, S.2
  • 63
    • 84907108944 scopus 로고
    • Comparison between dissociation and inhibition of association of DNA/anti-DNA complexes
    • Smeenk, R. J. T., Aarden, L. A. and van Oss, C. J. (1983). Comparison between dissociation and inhibition of association of DNA/anti-DNA complexes. Immunol. Commun. 12, 177-188.
    • (1983) Immunol. Commun. , vol.12 , pp. 177-188
    • Smeenk, R.J.T.1    Aarden, L.A.2    Van Oss, C.J.3
  • 64
    • 0000267310 scopus 로고
    • Versuch einer mathematischen Theorie der Koagulationskinetik kolloider Lösungen
    • von Smoluchowski, M. (1917). Versuch einer mathematischen Theorie der Koagulationskinetik kolloider Lösungen. Z. physik. Chemie. 92, 129-168.
    • (1917) Z. Physik. Chemie. , vol.92 , pp. 129-168
    • Von Smoluchowski, M.1
  • 67
    • 0028498176 scopus 로고
    • Linkage between ζ-potential and electron-donicity of charged polar surfaces
    • Wu, W., Giese, R. F. and van Oss, C. J. (1994). Linkage between ζ-potential and electron-donicity of charged polar surfaces. Colloids Surfaces A. 83, 241-262.
    • (1994) Colloids Surfaces A , vol.83 , pp. 241-262
    • Wu, W.1    Giese, R.F.2    Van Oss, C.J.3


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