An analysis of analyte-receptor binding kinetics for biosensor applications: influence of the fractal dimension on the binding rate coefficient.
The diffusion-limited binding kinetics of analyte in solution to receptor immobilized on a biosensor surface is analysed within a fractal framework. Both a single- as well as a dual-fractal analysis are utilized. Antigen-antibody and analyte-receptor systems are analysed. For the antigen-antibody and analyte-receptor systems where a single- or a dual-fractal analysis was used, it is of interest to note that the binding rate coefficient and the fractal dimension exhibit changes in the same direction. The binding rate coefficient expressions obtained as a function of the fractal dimension indicate the high sensitivity of the binding rate coefficient with respect to the fractal dimension. For example, for a single-fractal analysis and for the binding of (a) 1 microM BSA in solution to the anti-BSA-protein fused to a biosensor surface, and for (b) the binding of m-xylene-saturated STE buffer solution to the microorganism immobilized to the fiber-optic end and covered with a polycarbonate membrane, the orders of dependence of the binding rate coefficient on the fractal dimension were 5.535 and 3.314, respectively. This emphasizes the importance of the degree of heterogeneity on the biosensor surface and its impact on the binding rate coefficient, k. This high sensitivity is also indicated for a dual-fractal analysis, at least for the binding rate coefficient, k2. For example, during regeneration runs and for the binding of polymerase chain-reaction amplified DNA in solution to DNA capture protein immobilized on a fiber-optic biosensor, the order of dependence of k2 on Df2 was 3.399. The fractional order of dependence of the binding rate coefficient(s) on the fractal dimension(s) further reinforces the fractal nature of the system. The binding rate coefficient expressions developed as a function of the fractal dimension for both single-fractal analysis and dual-fractal analysis systems are of particular value since they provide a means to better control biosensor performance by linking it to the heterogeneity on the surface. Also, the importance of the nature of the surface on biosensor performance is emphasized in a quantitative sense.
Sadana
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Chemical Engineering Department, University of Mississippi 38677-9740, USA.
D000937:Antigen-Antibody Reactions; D001667:Binding, Competitive; D015374:Biosensing Techniques; D004058:Diffusion; D005336:Fiber Optic Technology; D017709:Fractals; D007700:Kinetics; D055100:Optical Fibers; D011956:Receptors, Cell Surface / Q000378:metabolism*
D011956:Receptors, Cell Surface