Abstract
Induced fit and conformational selection are two dominant binding mechanisms in biology. Although induced fit has been widely accepted by supramolecular chemists, conformational selection is rarely studied with synthetic systems. In the present research, we report a macrocyclic host whose binding mechanism is unambiguously assigned to conformational selection. The kinetic and thermodynamic aspects of this system are studied in great detail. It reveals that the kinetic equation commonly used for conformational selection is strictly followed here. In addition, two mathematical models are developed to determine the association constants of the same guest to the two host conformations. A “conformational selectivity factor” is defined to quantify the fidelity of conformational selection. Many details about the kinetic and thermodynamic aspects of conformational selection are revealed by this synthetic system. The conclusion and the mathematical models reported here should be helpful in understanding complex molecular recognition in both biological and synthetic systems.
Highlights
Induced fit and conformational selection are two dominant binding mechanisms in biology
In textbooks, induced fit, which was proposed by Koshland in 19585, is the dominant concept that has often been invoked to explain the conformational changes in molecular recognition
Conformational selection has been widely accepted to explain allostery8 and signal transduction9 in nature; the research on protein folding indicates that proteins exist as conformational ensembles10, and conformational selection may be a dominant mechanism in ligand binding of certain proteins11
Summary
Induced fit and conformational selection are two dominant binding mechanisms in biology. Conformational selection has been widely accepted to explain allostery and signal transduction in nature; the research on protein folding indicates that proteins exist as conformational ensembles, and conformational selection may be a dominant mechanism in ligand binding of certain proteins. Conformational selection has been widely accepted to explain allostery and signal transduction in nature; the research on protein folding indicates that proteins exist as conformational ensembles, and conformational selection may be a dominant mechanism in ligand binding of certain proteins11 The differentiation between these two mechanisms is often trivial but important for understanding biological processes. Recent studies indicate that an increase in kobs with [L] is not unequivocal evidence of the induced fit model14 This further complicates the assignments of the binding mechanism.
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