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24 August 2010 Measuring binding kinetics of biomolecular interactions using a localized surface plasmon couple fluorescence fiber optic biosensor
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Abstract
In this study, we describe a novel method for analyzing protein-protein binding kinetics at ultra-low concentration (1 pg/mL) using a localized surface plasmon coupled fluorescence fiber-optic biosensor (LSPCF-FOB). The association and dissociation rate constants, ka and kd, respectively, for the binding kinetics of the mouse IgG/ anti-mouse IgG interaction have been calculated to be ka = (5.9928±3.1540)x106 M-1s-1 and kd = (1.0587±0.5572)x10-3 s-1. The theoretical basis of this analytical approach is a rapid-mixing model integrated with a two-compartment model; has been experimentally verified in this study as well. The LSPCF-FOB provides a potentially alternative option for characterizing the interaction of biomolecules at ultra-low concentrations.
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Ying-Feng Chang, Jo-Ping Hsieh, Li-Chen Su, Ying-Chang Li, Cheng-Chung Lee, and Chien Chou "Measuring binding kinetics of biomolecular interactions using a localized surface plasmon couple fluorescence fiber optic biosensor", Proc. SPIE 7759, Biosensing III, 77590H (24 August 2010); doi: 10.1117/12.863621; https://doi.org/10.1117/12.863621
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