PubMed1997
The diffusion-limited binding kinetics of antigen-antibody, ligand-receptor, analyte-receptorless systems for biosensor applications is analyzed within a fractal framework. The analysis presented applies equally well to these types of systems. For example, for the binding of 2-(p-toluidiny)-naphthalene-6-sulfonic acid (2,6-TNS) to beta-cyclodextrin (ligand-receptor system) immobilized on a fiber-optic base inclusate biosensor, an increase in temperature from 4 to 30 degrees C leads to an increase in the fractal dimension, D1 and to a decrease in the binding rate coefficient, k1. For the binding of TRITC-labeled low-density proteins (LDL) directly to an optical fiber-based sensor (analyte-receptorless system), an increase in the LDL concentration from 5 to 50 micrograms ml-1 in solution leads to a decrease in the fractal dimension, D1 and to an increase in the binding rate coefficient, k1. Also, during the binding of human chorionic gonadotropin (hCG) to anti-hCG antibody immobilized on a HPLC column (antigen-antibody system), an increase in temperature from 4 to 50 degrees C leads to an increase in the fractal dimension, D1 and in the binding rate coefficient. k1. The different examples analyzed and presented together for the three different types of systems provide one means of a 'unified analysis,' and a method by which the forward binding rate coefficient, k1 may be controlled, that is, by changing the fractal dimension or 'disorder' on the surface. The analysis should assist in improving the stability, sensitivity, and response time of biosensors wherein different types of binding systems are utilized in the analysis method. More-or-less all of the treatment presented should be applicable to the above types of binding systems occurring in non-biosensor applications also. However, the single-fractal analysis is unable to describe the data over the full time course of some of the experiments.