Compensation for loss of ligand activity in surface plasmon resonance experiments.
The determination of equilibrium binding constants is an important aspect of the analysis of protein-protein interactions. In recent years surface plasmon resonance experiments (e.g., with a BIAcore instrument) have provided a valuable experimental approach to determining such constants. The standard method is based on measuring amounts of analyte bound at equilibrium for different analyte concentrations. During the course of a typical surface plasmon resonance experiment the measured equilibrium levels for a given analyte concentration often decrease. This appears to be due to a loss of activity of the protein coupled to the sensor chip or other phenomena. The loss in signal can lead to an erroneous determination of the equilibrium constant. A data analysis approach is introduced that aims to compensate for the loss of activity so that its influence on the results of the experiments is reduced.
Center for Systems, Communications and Signal Processing, Eric Jonsson School of Electrical Engineering and Computer Science, University of Texas at Dallas, Richardson 75083-0688, USA.
Raimund J
RJ
Ober
E Sally
ES
Ward
D007140:Immunoglobulin Fab Fragments; D007700:Kinetics; D008024:Ligands; D009113:Muramidase / Q000276:immunology / Q000378:metabolism*; D020349:Surface Plasmon Resonance
D007140:Immunoglobulin Fab Fragments; D008024:Ligands; D009113:Muramidase