Thermodynamic Analysis of Antigen–Antibody Binding Using Biosensor Measurements at Different Temperatures

Zeder‐Lutz, Gabrielle; Zuber, Emmanuel; Witz, Jean‐François; Regenmortel, M.H.V. Van

doi:10.1006/abio.1996.9999

Cited by 81 publications

(50 citation statements)

References 31 publications

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“…(45) Recently, thermodynamic parameters (⌬H and ⌬G) have been obtained by analysis of k a and k d at different temperatures. (46) Linear transformation.…”

Section: What's New?mentioning

confidence: 99%

Instrumental biosensors: new perspectives for the analysis of biomolecular interactions

1999

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“…(45) Recently, thermodynamic parameters (⌬H and ⌬G) have been obtained by analysis of k a and k d at different temperatures. (46) Linear transformation.…”

Section: What's New?mentioning

confidence: 99%

Instrumental biosensors: new perspectives for the analysis of biomolecular interactions

1999

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“…In the remaining 20 cases both enthalpy and entropy favor association [13]. At different temperatures, the leading driving force of protein-protein interaction in one complex can be different [40]. In most cases, the effects of enthalpy and entropy are opposite.…”

Section: Thermodynamics and Kinetics Of Protein-protein Interactionsmentioning

confidence: 99%

Protein‐protein interactions as a target for drugs in proteomics

et al. 2003

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Protein-protein interactions play a central role in numerous processes in the cell and are one of the main fields of functional proteomics. This review highlights the methods of bioinformatics and functional proteomics of protein-protein interaction investigation. The structures and properties of contact surfaces, forces involved in protein-protein interactions, kinetic and thermodynamic parameters of these reactions were considered. The properties of protein contact surfaces depend on their functions. The contact surfaces of permanent complexes resemble domain contacts or the protein core and it is reasonable to consider such complex formation as a continuation of protein folding. Characteristics of contact surfaces of temporary protein complexes share some similarities with active sites of enzymes. The contact surfaces of the temporary protein complexes have unique structure and properties and they are more conservative in comparison with active site of enzymes. So they represent prospective targets for a new generation of drugs. During the last decade, numerous investigations were undertaken to find or design small molecules that block protein dimerization or protein(peptide)-receptor interaction, or, on the contrary, to induce protein dimerization.

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“…As a first step in analysis of their thermodynamics, we use BIACORE SPR technology for real-time monitoring of the association and dissociation kinetics of the H10 and H26 complexes with HEL at varying temperatures (Karlsson and Falt, 1997;Zeder-Lutz et al, 1997;Roos et al, 1998;Roos and Karlsson, 1999). Here we demonstrate for the first time that temperature differentially impacts the encounter and docking step of these antigenantibody complexes, and that the relative impact on each step differs for the two antibodies.…”

Section: Introductionmentioning

confidence: 99%

Temperature differentially affects encounter and docking thermodynamics of antibody–antigen association

Lipschultz

Yee

Srinivasan

et al. 2002

J of Molecular Recognition

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Using BIACORE SPR, we have examined the mechanism of temperature effects on the binding kinetics of two closely related antibody Fabs (H10 and H26) which recognize coincident epitopes on hen egg-white lysozyme (HEL), and whose association and dissociation kinetics are best described by the two-step conformational change model which we interpret as molecular encounter and docking. Time-course series data obtained at a series of six temperatures (6, 10, 15, 25, 30 and 37 degrees C) showed that temperature differentially affects the rate constants of the encounter and docking steps. Docking is more temperature-sensitive than the encounter step, and energetically less favorable at higher temperatures. At elevated temperatures, the time required for docking is longer and the apparent increase in off-rate reflects the greater proportion of the molecules failing to dock and remaining in the less stable encounter state. As a consequence, distribution of free energy change between the encounter and docking steps is altered. At physiological temperature (37 degrees C) the docking step of the H26 complex is energetically unfavorable and most complexes essentially do not dock. There is a significant decrease in total free energy change of the H26 complex at higher temperatures. Elevated temperature changes the rate-limiting step of H26--HEL association from the encounter to the docking step, but not that of H10--HEL. Our results indicate that the mechanism by which elevated temperature reduces the affinities of antigen--antibody complexes is to decrease the net docking rate, and/or stability of the docked complex; at higher temperatures, a smaller proportion of the complexes actually anneal to a more stable docked state. This mechanism may have broad applicability to other receptor--ligand complexes.

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Thermodynamic Analysis of Antigen–Antibody Binding Using Biosensor Measurements at Different Temperatures

Cited by 81 publications

References 31 publications

Instrumental biosensors: new perspectives for the analysis of biomolecular interactions

Instrumental biosensors: new perspectives for the analysis of biomolecular interactions

Protein‐protein interactions as a target for drugs in proteomics

Temperature differentially affects encounter and docking thermodynamics of antibody–antigen association

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