Antigen-antibody binding kinetics for biosensor applications. A dual-fractal analysis.
The diffusion-limited binding kinetics of antigen (or antibody) in solution to antibody (or antigen) immobilized on a biosensor surface is analyzed within a fractal framework. The fit obtained by a dual-fractal analysis is compared with that obtained from a single-fractal analysis. In some cases, the dual-fractal analysis provides an improved fit when compared with a single-fractal analysis. This was indicated by the regression analysis provided by Sigmaplot (San Rafael, CA). These examples are presented. It is of interest to note that the state of disorder (or the fractal dimension) and the binding rate coefficient both increase (or decrease, a single example is presented for this case) as the reaction progresses on the biosensor surface. For example, for the binding of monoclonal antibody MAb 49 in solution to surface-immobilized antigen, a 90.4% increase in the fractal dimension (Df1 to Df2) from 1.327 to 2.527 leads to an increase in the binding rate coefficient (k1 to k2) by a factor of 9.4 from 11.74 to 110.3. The different examples analyzed and presented together provide a means by which the antigen-antibody reactions may be better controlled by noting the magnitude of the changes in the fractal dimension and in the binding rate coefficient as the reaction progresses on the biosensor surface.
Sadana
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Chemical Engineering Department, University of Mississippi 38677-9740, USA. cmsadana@olemiss.edu
Suturia
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D000937:Antigen-Antibody Reactions; D015374:Biosensing Techniques; D005336:Fiber Optic Technology; D017709:Fractals; D007700:Kinetics