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Biophysical Journal 58: 1235-1249 (1990)
© 1990 the Biophysical Society

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Binding of a monoclonal antibody and its Fab fragment to supported phospholipid monolayers measured by total internal reflection fluorescence microscopy.

M L Pisarchick and N L Thompson

Department of Chemistry, University of North Carolina, Chapel Hill 27599-3290.

ABSTRACT

The association of an anti-dinitrophenyl monoclonal antibody and its Fab fragment with supported phospholipid monolayers composed of a mixture of dipalmitoylphosphatidylcholine and dinitrophenyl-conjugated dipalmitoylphosphatidylethanolamine has been characterized with total internal reflection fluorescence microscopy. The surface densities of bound antibodies were measured as a function of the antibody and Fab solution concentrations, and as a function of the solution concentration of dinitrophenylglycine. The apparent association constant of Fab fragments with surface-associated haptens was approximately 10-fold lower than the association constant for haptens in solution, and the apparent surface association constant for intact antibodies was only approximately 10-fold higher than the constant for Fab fragments. Data analysis with simple theoretical models indicated that, at most antibody surface densities, 50-90% of membrane-associated intact antibodies were attached to the surface by two antigen binding sites.




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H. Jung, T. Yang, M. D. Lasagna, J. Shi, G. D. Reinhart, and P. S. Cremer
Impact of Hapten Presentation on Antibody Binding at Lipid Membrane Interfaces
Biophys. J., April 15, 2008; 94(8): 3094 - 3103.
[Abstract] [Full Text] [PDF]


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Copyright © 1990 by the Biophysical Society.