TY - GEN
T1 - Estimation of kinetic rate constants from surface plasmon resonance experiments
AU - Evans, Neil D.
AU - Lowe, David
AU - Briggs, David
AU - Higgins, Robert
AU - Bentall, Andrew
AU - Ball, Simon
AU - Mitchell, Daniel
AU - Zehnder, Daniel
AU - Chappell, Michael J.
N1 - Copyright:
Copyright 2013 Elsevier B.V., All rights reserved.
PY - 2010
Y1 - 2010
N2 - In order to characterise antibody binding characteristics it is necessary to determine reaction constants from quantitative measurements of the process. Surface plasmon resonance (SPR) provides convenient real-time measurement of the reaction that enables subsequent estimation of the reaction constants. Two models are considered that represent the binding reaction in the presence of transport effects. One of these models, the effective rate constant approximation, can be derived from the other applying a quasi-steady state assumption. Uniqueness of the reaction constants with respect to SPR measurements is considered via a structural identifiability analysis. It is shown that the effective rate constant model is unidentifiable, unless the analyte concentration is known, while the full model is structurally globally identifiable provided association and dissociation phases are considered. Both models provide comparable estimates for the unknown rate constants for a commercial anti-A monoclonal IgM experiment.
AB - In order to characterise antibody binding characteristics it is necessary to determine reaction constants from quantitative measurements of the process. Surface plasmon resonance (SPR) provides convenient real-time measurement of the reaction that enables subsequent estimation of the reaction constants. Two models are considered that represent the binding reaction in the presence of transport effects. One of these models, the effective rate constant approximation, can be derived from the other applying a quasi-steady state assumption. Uniqueness of the reaction constants with respect to SPR measurements is considered via a structural identifiability analysis. It is shown that the effective rate constant model is unidentifiable, unless the analyte concentration is known, while the full model is structurally globally identifiable provided association and dissociation phases are considered. Both models provide comparable estimates for the unknown rate constants for a commercial anti-A monoclonal IgM experiment.
KW - Binding affinity
KW - Biomedical systems
KW - Parameter estimation
KW - Structural identifiability
KW - Surface plasmon resonance
KW - Surface-volume reactions
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U2 - 10.1049/ic.2010.0300
DO - 10.1049/ic.2010.0300
M3 - Conference contribution
AN - SCOPUS:84877801344
SN - 9781846000386
T3 - IET Seminar Digest
SP - 311
EP - 316
BT - UKACC International Conference on CONTROL 2010
T2 - UKACC International Conference on CONTROL 2010
Y2 - 7 September 2010 through 10 September 2010
ER -