Journal of Colloid and Interface Science, Vol.213, No.2, 465-478, 1999
A single and a dual-fractal analysis of analyte-receptor binding kinetics for surface plasmon resonance biosensor applications
The diffusion-limited binding kinetics of analyte in solution to either a receptor immobilized on a surface or to a receptorless surface is analyzed within a fractal framework for a surface plasmon resonance biosensor, The data is adequately described by a single- or a dual-fractal analysis. Initially, the data was modeled by a single-fractal analysis. If an inadequate fit was obtained then a dual-fractal analysis was utilized. The regression analysis provided by Sigmaplot (32) was used to determine if a single fractal analysis is sufficient or if a dual-fractal analysis is required. In general, it is of interest to note that the binding rate coefficient and the fractal dimension exhibit changes in the same direction (except for a single example) for the analyte-receptor systems analyzed. Binding rate coefficient expressions as a function of the fractal dimension developed for the analyte-receptor binding systems indicate, in general, the high sensitivity of the binding rate coefficient on the fractal dimension when both a single- and a dual-fractal analysis is used. For example, for a single-fractal analysis : and for the binding of human endothelin-l (ET-I) antibody in solution to ET-1(15-21).BSA immobilized on a surface plasmon resonance (SPR) surface (33), the order of dependence of the binding rate coefficient, k, on the fractal dimension, D-f, is 6.4405. Similarly, for a dual-fractal analysis and for the binding of 10(-6) to 10(-4) M bSA in solution to a receptorless surface (direct binding to SPR surface) (41) the order of dependence of k(1) and k(2) on D-f1 and D-f2 were -2.356 and 6.241, respectively, Binding rate coefficient expressions are also developed as a function of the analyte concentration in solution. The binding rate coefficient expressions developed as a function of the fractal dimension(s) are of particular value since they provide a means to better control SPR biosensor performance by linking it to the degree of heterogeneity that exists on the SPR biosensor surface.