PMC:7152911 / 73517-75240 JSONTXT

{"target":"https://pubannotation.org/docs/sourcedb/PMC/sourceid/7152911","sourcedb":"PMC","sourceid":"7152911","source_url":"https://www.ncbi.nlm.nih.gov/pmc/7152911","text":"2.4 Thermodynamics of pathogen-biorecognition element binding reactions\nWhile the rate of biosensor response is typically governed by a mass transfer-limited heterogeneous reaction between the immobilized biorecognition element and target species, the net change in the biosensor response is dependent on the reaction thermodynamics. The binding affinity between a biorecognition element and target species, such as an antibody and antigen, is often reported in terms of a dissociation constant (K D), which has units of M. While the value of K D, solution = 1 nM provides a reasonable estimate for biosensor design considerations, such as understanding the mass transfer limitations associated with biosensor response (Squires et al. 2008), the binding affinity of antibodies can vary by orders of magnitude depending on the pathogen of interest and the clonality of the antibody. One important consideration when immobilizing biorecognition elements is potential effects of immobilization on binding affinity to the target. Traditionally, K D is obtained from a kinetic or thermodynamic analysis. Kinetic analyses measure association and dissociation rate constants (k a and k d, respectively) and enable calculation of K D as k d/k a. Thermodynamic analyses, such as calorimetric techniques, measure the binding enthalpy and entropy, which in turn provides the standard Gibbs free energy of the reaction (ΔG°), and thus, K A = K D −1 though the expression K A = exp(-ΔG°/RT), where R is the gas constant and T is the temperature. A detailed discussion of the kinetics and thermodynamics of biorecognition element-target binding reactions for solution- and surface-based biosensors is provided in Supporting 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