Surface plasmon resonance based biosensors are being used to define the kinetics of a wide variety of macromolecular interactions. As the popularity of this approach grows, experimental design and data analysis methods continue to evolve. These advances are making it possible to accurately define th
Reliable determination of binding affinity and kinetics using surface plasmon resonance biosensors
β Scribed by Peter Schuck
- Publisher
- Elsevier Science
- Year
- 1997
- Tongue
- English
- Weight
- 690 KB
- Volume
- 8
- Category
- Article
- ISSN
- 0958-1669
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β¦ Synopsis
Progress has been made in the identification of experimental and analytical procedures that allow for a more reliable determination of equilibrium and kinetic constants. Possible origins of the frequently observed deviations of the measured binding progress from that expected for chemical binding of pseudo-first order, and appropriate experimental controls have been proposed. Improved analytical approaches include the application of global analysis and analytical corrections for the influence of mass transport.
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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
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. Initiall