Enhanced fluorescence of epicocconone in surfactant assemblies as a consequence of depth-dependent microviscosity

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Enhanced fluorescence of epicocconone in surfactant assemblies as a consequence of depth-dependent microviscosity

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Title: Enhanced fluorescence of epicocconone in surfactant assemblies as a consequence of depth-dependent microviscosity
Author: PANDA, D; KHATUA, S; DATTA, A
Abstract: The extents of fluorescence enhancement of epicocconone are found to be different in the micelles of the surfactants sodium dodecyl sulfate (SDS) and Triton X100 (TX 100). A decrease in fluorescence, observed in the cationic cetyltrimethylammonium bromide (CTAB) micelles, is rationalized by the formation of anions of the fluorophore at the Stern layer. To understand the difference in the effects of SDS and TX 100, the nature of the excited-state process in the fluorophore has been investigated by fluorescence spectroscopy, supported by complementary quantum chemical calculations. The excited-state dynamics of epicocconone is found to depend on polarity and viscosity of the medium, with a more pronounced dependence on viscosity. An inspection of the molecular orbitals involved in the electronic absorption of the molecule reveals the possibility of photoisomerization, which conforms to the observed solvent dependence of the fluorescence spectral properties. An apparent mismatch between trends observed in steady-state spectra and those in temporal decays indicates a significant contribution of an ultrafast component, which cannot be detected in the time resolution of our instrument. The viscosity dependence of the fluorescence quantum yields provides an explanation for the difference in the extents of fluorescence enhancement in the two micelles, in the light of location of the fluorophore at different depths of the micelle. The enhancement of fluorescence, with an unchanged fluorescence maximum, opens up the possibility that the fluorophore could be a useful dual emitting marker for fluorescence microscopy of heterogeneous systems, as the fluorescence of protein-bound epicocconone has been previously reported to be significantly red-shifted.
URI: http://dx.doi.org/10.1021/jp065226o
http://dspace.library.iitb.ac.in/xmlui/handle/10054/3824
http://hdl.handle.net/10054/3824
Date: 2007


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