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Abstract: Abstract: The complex nature of the structure of the anticoagulant warfarin is reflected in the diversity of binding modes observed in warfarin - protein recognition systems. A series of theoretical, 1H-NMR and steady state and time resolved fluorescence spectroscopic studies, have been used to establish correlations between the molecular environment provided by various solvent systems and the relative concentrations of the various members of warfarin's ensemble of isomers. A consequence of these observations is that the judicious choice of solvent system or molecular environment of warfarin allows for manipulation of the position of the equilibrium between isomeric structures such as the hemiacetal and open phenol-keto forms, the latter even possible in a deprotonated form, where in each case unique spectroscopic properties are exhibited by the respective structures. Collectively, warfarin's capacity to adapt its structure as a function of environment in conjunction with the fluorescence behaviours of the various isomers together provide an environment-dependent molecular switch with reporter properties, which allows for the simultaneous detection of warfarin in different states with lifetimes spanning the range < 0.10 - 5.5 ns. These characteristics are here used to examine warfarin binding domains in a series of materials (solvents, protein, inorganic matrix and synthetic polymer). Moreover, these studies demonstrate the potential for using warfarin, or other switchable analogues thereof, as a tool for studying molecular level characteristics, for example local dielectricity. Copyright © 2010 John Wiley & Sons, Ltd
Template and target information: warfarin
Author keywords: Warfarin, fluorescence, fluorescence lifetimes, organic solvents, molecular recognition, molecular probe, molecularly imprinted polymer, human serum albumin, HSA, colloidal silica, TCSPC