Title
Structural identifiability of surface binding reactions involving heterogeneous analyte: Application to surface plasmon resonance experiments
Abstract
Binding affinities are useful measures of target interaction and have an important role in understanding biochemical reactions that involve binding mechanisms. Surface plasmon resonance (SPR) provides convenient real-time measurement of the reaction that enables subsequent estimation of the reaction constants necessary to determine binding affinity. Three models are considered for application to SPR experiments-the well-mixed Langmuir model and two models 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 by 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 models are structurally unidentifiable unless the sample concentration is known. The models are also considered for analytes with heterogeneity in the binding kinetics. This heterogeneity further confounds the identifiability of key parameters necessary for reliable estimation of the binding affinity.
Year
DOI
Venue
2013
10.1016/j.automatica.2012.09.015
Automatica
Keywords
Field
DocType
Biomedical systems,Structural identifiability,Surface plasmon resonance,Surface-volume reactions,Binding affinity,System identification
Reaction rate constant,Surface plasmon resonance,Biological system,Identifiability,Control theory,Ligand (biochemistry),Receptor–ligand kinetics,Langmuir adsorption model,Analyte,Affinities,Mathematics
Journal
Volume
Issue
ISSN
49
1
0005-1098
Citations 
PageRank 
References 
3
0.57
5
Authors
8
Name
Order
Citations
PageRank
N. D. Evans130.57
H. A. J. Moyse230.57
D. Lowe330.57
D. Briggs4101.10
R. Higgins530.57
D. Mitchell630.57
D. Zehnder741.28
Michael J. Chappell8407.97