The green fluorescent protein (GFP) chromophore has been anchored to β-cyclodextrin (βCD) via a copper(I)-catalyzed azide-alkyne cycloaddition. The photophysical properties of this new GFP-CD derivative have been evaluated, showing the formation of a self-inclusion complex and enhancement of fluorescence of the GFP-chromophore covalently bound to the βCD. This enhancement of fluorescence by encapsulation and hence fixation of the chromophore in a binding pocket mimics the effect exerted by the natural protein environment.
<beta>-Cyclodextrin as a mimetic of the natural GFP-chromophore environment / M. Cacciarini;* M. B. Nielsen; E. M. de Castro; L. Marinescu; M. Bols. - In: TETRAHEDRON LETTERS. - ISSN 0040-4039. - STAMPA. - 53:(2012), pp. 973-976. [10.1016/j.tetlet.2011.12.053]
-Cyclodextrin as a mimetic of the natural GFP-chromophore environment
CACCIARINI, MARTINA;
2012
Abstract
The green fluorescent protein (GFP) chromophore has been anchored to β-cyclodextrin (βCD) via a copper(I)-catalyzed azide-alkyne cycloaddition. The photophysical properties of this new GFP-CD derivative have been evaluated, showing the formation of a self-inclusion complex and enhancement of fluorescence of the GFP-chromophore covalently bound to the βCD. This enhancement of fluorescence by encapsulation and hence fixation of the chromophore in a binding pocket mimics the effect exerted by the natural protein environment.
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