Determination of kinetic rate and equilibrium binding constants for macromolecular interactions: a critique of the surface plasmon resonance literature
References and recommended reading (22)
Surface Plasmon Resonance for Detection and Measurement of Antibody-Antigen Affinity and Kinetics
Curr Opin Immunol
(1993)- et al.
Interactions between SH2 Domains and Tyrosine-Phosphorylated Platelet-Derived Growth Factor β-Receptor Sequences: Analysis of Kinetic Parameters by a Novel Biosensor Approach
Mol Cell Biol
(1993) - et al.
Thermodynamic Analysis of an Antibody Functional Epitope
Biochemistry
(1993) - et al.
Nature of the Interaction of Heparin with Acidic Fibroblast Growth Factor
Biochemistry
(1993) - et al.
Binding Kinetics of Antigen by Immobilized Antibody: Influence of Reaction Order and External Diffusional Limitations
Biosensors Bioelectronics
(1992) - et al.
The Resonant Mirror: A Novel Optical Biosensor for Direct Sensing of Biomolecular Interactions Part I: Principle of Operation and Associated Instrumentation
Biosensors Bioelectronics
(1993) - et al.
The Difference Interferometer: A Highly Sensitive Optical Probe for Quantification of Molecular Surface Concentration
Biosensors Bioelectronics
(1994) - et al.
Real Time Analysis of Antibody-Antigen Reaction Kinetics
Scand J Immunol
(1992) - et al.
Kinetic Analysis of Recombinant Antibody-Antigen Interactions: Relation between Structural Domains and Antigen Binding
Biotechnology
(1992) - et al.
A Biosensor Approach to Probe the Structure and Function of the p85a Subunit of the Phosphatidylinositol 3-Kinase Complex
J Biol Chem
(1993)
Monoclonal Antipeptide Antibodies: Affinity and Kinetic Rate Constants Measured for the Peptide and the Cognate Protein using a Biosensor Technology
Mol Immunol
Cited by (136)
Mathematical modeling of immunochromatographic test systems in a competitive format: Analytical and numerical approaches
2020, Biochemical Engineering Journal3.1 Surface analysis and biointerfaces: Vacuum and ambient in situ techniques
2017, Comprehensive Biomaterials IIReal-time label-free detection and kinetic analysis of Etanercept—Protein A interactions using quartz crystal microbalance
2017, Colloids and Surfaces B: BiointerfacesCitation Excerpt :Therefore, at lower concentrations, Enbrel® diffuses more readily towards and away from the biosensor surface resulting in greater kinetic rate constants with respect to higher Enbrel® concentrations (i.e., kon,1 > kon,2 and koff,1 > koff,2). This model is similar to that previously described by O’Shannessy [26] for explaining mass transport limitations of surface plasmon resonance (SPR) for the determination of the kinetic rate (kon, koff) and equilibrium (KA, KD) constants. Mass transport limitations highlighted in Fig. 4 explain the decrease of kon and koff as Enbrel® concentration increases (Table 1).
Analytical Ultracentrifugation and Its Role in Development and Research of Therapeutical Proteins
2015, Methods in EnzymologyCitation Excerpt :Initial clinical results suggested that the dose needed to be higher and this raised several questions as to the accuracy of the affinity measurements using surface plasmon resonance (SPR) technology. Although SPR has been one of the best methods to determine high-affinity-binding constants, the experimental design needs to be thoroughly explored because of many artifacts that can occur, mainly as the results of immobilizing of one of the reactants to the carboxymethyldextran on the gold surface used in SPR (O'Shannessy, 1994; Trilling, Harmsen, Ruigrok, Zuilhof, & Beekwilder, 2013). In order to address this issue, a competitive binding AUC method was developed.
High affinity anti-Internalin B VHH antibody fragments isolated from naturally and artificially immunized repertoires
2015, Journal of Immunological MethodsCitation Excerpt :The bi-phasic binding is thought to be a result of non-specific interactions which occur at higher concentrations. The KD value for the interaction between R3-26 and immobilized Internalin B was derived by fitting the data to a steady state model (O'Shannessy, 1994). This analysis allows the determination of the KD value but not the kon and koff values; hence these kinetic constants are not reported in the case of R3-26.