Interpolation method for accurate affinity ranking of arrayed ligand analyte interactions

Richard B.M. Schasfoort; Kiki Andree; Niels van der Velde; Alex van der Kooi; Ivan Stojanović; Leon W.M.M. Terstappen

doi:10.1016/j.ab.2016.01.023

Interpolation method for accurate affinity ranking of arrayed ligand analyte interactions

Richard B.M. Schasfoort^*, Kiki Andree, Niels van der Velde, Alex van der Kooi, Ivan Stojanović, Leon W.M.M. Terstappen

^*Corresponding author for this work

Research output: Contribution to journal › Article › Academic › peer-review

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Abstract

The values of the affinity constants (kd, ka, and KD) that are determined by label-free interaction analysis methods are affected by the ligand density. This article outlines a surface plasmon resonance (SPR) imaging method that yields high-throughput globally fitted affinity ranking values using a 96-plex array. A kinetic titration experiment without a regeneration step has been applied for various coupled antibodies binding to a single antigen. Globally fitted rate (kd and ka) and dissociation equilibrium (KD) constants for various ligand densities and analyte concentrations are exponentially interpolated to the KD at Rmax = 100 RU response level (KDR100).

Original language	English
Pages (from-to)	21-23
Journal	Analytical biochemistry
Volume	500
DOIs	https://doi.org/10.1016/j.ab.2016.01.023
Publication status	Published - 13 Feb 2016

Keywords

2023 OA procedure

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10.1016/j.ab.2016.01.023

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title = "Interpolation method for accurate affinity ranking of arrayed ligand analyte interactions",

abstract = "The values of the affinity constants (kd, ka, and KD) that are determined by label-free interaction analysis methods are affected by the ligand density. This article outlines a surface plasmon resonance (SPR) imaging method that yields high-throughput globally fitted affinity ranking values using a 96-plex array. A kinetic titration experiment without a regeneration step has been applied for various coupled antibodies binding to a single antigen. Globally fitted rate (kd and ka) and dissociation equilibrium (KD) constants for various ligand densities and analyte concentrations are exponentially interpolated to the KD at Rmax = 100 RU response level (KDR100).",

keywords = "2023 OA procedure",

author = "Schasfoort, {Richard B.M.} and Kiki Andree and {van der Velde}, Niels and {van der Kooi}, Alex and Ivan Stojanovi{\'c} and Terstappen, {Leon W.M.M.}",

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AU - Schasfoort, Richard B.M.

AU - Andree, Kiki

AU - van der Velde, Niels

AU - van der Kooi, Alex

AU - Stojanović, Ivan

AU - Terstappen, Leon W.M.M.

PY - 2016/2/13

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N2 - The values of the affinity constants (kd, ka, and KD) that are determined by label-free interaction analysis methods are affected by the ligand density. This article outlines a surface plasmon resonance (SPR) imaging method that yields high-throughput globally fitted affinity ranking values using a 96-plex array. A kinetic titration experiment without a regeneration step has been applied for various coupled antibodies binding to a single antigen. Globally fitted rate (kd and ka) and dissociation equilibrium (KD) constants for various ligand densities and analyte concentrations are exponentially interpolated to the KD at Rmax = 100 RU response level (KDR100).

AB - The values of the affinity constants (kd, ka, and KD) that are determined by label-free interaction analysis methods are affected by the ligand density. This article outlines a surface plasmon resonance (SPR) imaging method that yields high-throughput globally fitted affinity ranking values using a 96-plex array. A kinetic titration experiment without a regeneration step has been applied for various coupled antibodies binding to a single antigen. Globally fitted rate (kd and ka) and dissociation equilibrium (KD) constants for various ligand densities and analyte concentrations are exponentially interpolated to the KD at Rmax = 100 RU response level (KDR100).

KW - 2023 OA procedure

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DO - 10.1016/j.ab.2016.01.023

M3 - Article

SN - 0003-2697

VL - 500

SP - 21

EP - 23

JO - Analytical biochemistry

JF - Analytical biochemistry

ER -

Interpolation method for accurate affinity ranking of arrayed ligand analyte interactions

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Keywords

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