Method for estimating the single molecular affinity

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Schasfoort, R.B.M. and Lau de, W. and Kooi van der, A. and Clevers, H. and Engbers, G.H.M. (2012) Method for estimating the single molecular affinity. Analytical biochemistry, 421 . 794 - 796. ISSN 0003-2697

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Abstract:Affinity constants (kd, ka, and KD) can be determined by methods that apply immobilized ligands such as immunoassays and label-free biosensor technologies. This article outlines a new surface plasmon resonance (SPR) array imaging method that yields affinity constants that can be considered as the best estimate of the affinity constant for single biomolecular interactions. Calculated rate (kd and ka) and dissociation equilibrium (KD) constants for various ligand densities and analyte concentrations are extrapolated to the KD at the zero response level (KDR0). By applying this method to an LGR5-exo-Fc¿RSPO1-FH interaction couple, the KDR0 was determined as 3.1 nM.
Item Type:Article
Copyright:© 2012 Elsevier
Faculty:
Science and Technology (TNW)
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Link to this item:http://purl.utwente.nl/publications/81866
Official URL:http://dx.doi.org/10.1016/j.ab.2011.12.011
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Metis ID: 282485