A predictive approach using fractal analysis is presented for analyte-receptor binding and dissociation kinetics for biosensor applications. Data taken from the literature may be modeled, in the case of binding using a single-fractal analysis or a dual-fractal analysis. The dual-fractal analysis rep
A Single and a Dual-Fractal Analysis of Analyte-Receptor Binding Kinetics for Surface Plasmon Resonance Biosensor Applications
✍ Scribed by Anand Ramakrishnan; Ajit Sadana
- Publisher
- Elsevier Science
- Year
- 1999
- Tongue
- English
- Weight
- 160 KB
- Volume
- 213
- Category
- Article
- ISSN
- 0021-9797
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✦ Synopsis
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 dualfractal analysis is used. For example, for a single-fractal analysis and for the binding of human endothelin-1 (ET-1) 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.
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